You are on page 1of 185

Biochemistry for Dental Students

Biochemistry for Dental Students

(Theory and Practical)

Shreya Nigoskar MSc PhD

Associate Professor of Biochemistry College of Dental Sciences & Hospital, Rau, Indore (MP)

Biochemistry for Dental Students (Theory and Practical) Shreya Nigoskar MSc PhD Associate Professor of Biochemistry College



New Delhi

Published by

Jitendar P Vij

Jaypee Brothers Medical Publishers (P) Ltd

B-3 EMCA House, 23/23B Ansari Road, Daryaganj New Delhi 110 002, India Phones: +91-11-23272143, +91-11-23272703, +91-11-23282021, +91-11-23245672, Rel: 32558559

Fax: +91-11-23276490, +91-11-23245683


Visit our website:


  • 2/B, Akruti Society, Jodhpur Gam Road Satellite, Ahmedabad 380 015 Phones: +91-079-26926233, Rel: +91-079-32988717, Fax: +91-079-26927094 e-mail:

  • 202 Batavia Chambers, 8 Kumara Krupa Road Kumara Park East, Bangalore 560 001 Phones: +91-80-22285971, +91-80-22382956, Rel: +91-80-32714073, Fax: +91-80-22281761 e-mail:

  • 282 IIIrd Floor, Khaleel Shirazi Estate, Fountain Plaza Pantheon Road, Chennai 600 008 Phones: +91-44-28193265, +91-44-28194897, Rel: +91-44-32972089, Fax: +91-44-28193231 e-mail:

  • 4-2-1067/1-3, 1st Floor, Balaji Building, Ramkote Cross Road Hyderabad 500 095, Phones: +91-40-66610020, +91-40-24758498, Rel:+91-40-32940929, Fax:+91-40-24758499, e-mail:

  • No. 41/3098, B and B1, Kuruvi Building, St. Vincent Road Kochi 682 018, Kerala, Phones: 0484-4036109, +91-0484 2395739, +91-0484 2395740

  • 1-A Indian Mirror Street, Wellington Square Kolkata 700 013, Phones: +91-33-22451926, +91-33-22276404, +91-33-22276415, Rel: +91-33-32901926 Fax: +91-33-22456075, e-mail:

  • 106 Amit Industrial Estate, 61 Dr SS Rao Road Near MGM Hospital, Parel, Mumbai 400 012 Phones: +91-22-24124863, +91-22-24104532, Rel: +91-22-32926896 Fax: +91-22-24160828,


  • “KAMALPUSHPA” 38, Reshimbag Opp. Mohota Science College, Umred Road Nagpur 440 009 (MS) Phone: Rel: 3245220, Fax: 0712-2704275 e-mail:

Biochemistry for Dental Students

© 2007, Jaypee Brothers Medical Publishers

All rights reserved. No part of this publication should be reproduced, stored in a retrieval system, or transmitted in any form or by any means: electronic, mechanical, photocopying, recording, or otherwise, without the prior written permission of the author and the publisher.

This book has been published in good faith that the material provided by author is original. Every effort is made to ensure accuracy of material, but the publisher, printer and author will not be held responsible for any inadvertent error(s). In case of any dispute, all legal matters are to be settled under Delhi jurisdiction only.

First Edition: 2007 ISBN 81-8448-049-0

Typeset at JPBMP typesetting unit Printed at Rajkamal

'kkafr Lo:ik; fon~egs] Hkkxor Js"Bk; f/kefg] rUuksa ekr±M izpksn;kr~

Dedicated to my Gurumaharaj Shri Nana Maharaj Taranekar

'kkafr Lo:ik; fon~egs] Hkkxor Js"Bk; f/kefg] rUuksa ekr±M izpksn;kr~ Dedicated to my Gurumaharaj Shri Nana Maharaj

and All the students who have inspired and encouraged me


Publishing of this book Biochemistry for Dental Students was not a long cherished dream like other authors but a spontaneous thought. While working as a Lecturer in Dept of Physiology and Biochemistry in College of Dental Sciences and Hospital in the year 2004, I met an unfortunate road accident and was in bed suffering from major head injury and a fractured limb. Neither I nor my kith and kin were sure that I would be even able to stand on my feet again. Before, the aforesaid miserable span of my life began, the librarian Mr Ravish Verma, had told me that, there is no adequate study material available in biochemistry for students of BDS first year although in the past few years, a number of textbooks in biochemistry have been published, primarily for students of medicine but none for students of dentistry. He suggested me to inscribe a book which could be of sufficient use to the students of not only this institute but of every renowned university in India. I am extremely grateful to him for his valuable advice. When, I fully recovered and joined the college, I initiated and completed the work and the editorial board of M/s Jaypee Brothers Medical Publishers (P) Ltd. New Delhi, became ready to publish the book. This book has been written to meet the needs of dental students in biochemistry, theory as well as practicals, while compiling, this book, I have consulted several syllabi so as to cover all the topics prescribed for BDS students of various universities. This is my first effort and may not be without errors, I request the teachers as well as students to send me their precious comments so that I can enhance the matter as well as manner of the book.

Shreya Nigoskar


First and foremost, I thank to the supreme power God, for giving me energy, inspiration and courage to complete this arduous task. Without His blessing nothing would have been possible.

  • I express my sincere gratitude to Mr Ajit Jhavar, Chairman, College of Dental Sciences

and Hospital, Dr HC Neema, Dean, College of Dental Sciences and Hospital, Dr HC Gupta, professor emeritus, Dept of Physiology and Biochemistry, College of Dental Sciences and

Hospital, Rau (Indore) for their constant support and encouragement.

  • I owe deep debt of gratitude to Dr (Mrs) Meena Verma, Professor and Head of Dept of

Biochemistry, MGM Medical College, Indore, for her constant encouragement in my academic pursuits. How can I put in words my gratitude to express my feelings for my parents, Mr MM Dixit and Mrs Madhuri Dixit, for bringing me up to this stage. It is not possible for me to express thanks to them in words as their good wishes and efforts for me can never be delineated. My limited vocabulary compels me to use all superlatives, which two members of my family deserve for this cooperation and association, my son Master Suryansh Nigoskar, who suffered a lot, during the inscription of the book, but never complained and my husband Mr Manoj Nigoskar who was beside me, throughout the period of the work. The value of their sincerity towards me cannot be measured on chart; because without their encouragement

and co-operation, this book could never have been published.





  • 1. ...........................................................................................................................



  • 2. ........................................................................................................................................



  • 3. .....................................................................................................................................


Amino Acids

  • 4. ............................................................................................................................



  • 5. .....................................................................................................................................


  • 6. Digestion, Absorption and Metabolism of Carbohydrates


  • 7. Digestion, Absorption and Metabolism of Lipids



  • 8. Digestion, Absorption and Metabolism of Proteins



  • 9. .................................................................................................................................


  • 10. Minerals: The Inorganic Elements



  • 11. ................................................................................................................................





  • 12. .......................................................................................................................



  • 13. ......................................................................................................................................



  • 14. ...................................................................................................................................



  • 15. ........................................................................................................................................





Life itself is full of a mystery which is tried to be solved by a chemistry which is termed as biochemistry. Biochemistry, it would like to introduce itself and to tell you something about it. It will not only be interesting but useful too. It is a secondary branch of a huge tree in a huge garden, i.e. in the garden of knowledge, there is a tree of Dental Science and Physiology and it is one of the primary branches of this tree and has many secondary branches including itself. The origin of biochemistry goes back to eighteenth century with Levostier’s explanation of respiration as biological oxidation of food and the experiments that showed that living matter contained proteins, carbohydrates and fats not found in mineral sources. At the turn of century, many scientists settled various facts. Such as establishment of structure of carbohydrates and protein and recognition of specificity of enzyme action by Emil Fischer and exploitation by Harden and Young of the accidental observation by Buchner brothers that a cell free extract of yeast could ferment glucose with production of alcohol. In this way the development of biochemistry continued. It was termed as biochemistry for the first time by Carl Neuberg in 1903. Biochemistry broadly deals with chemistry of life and living processes. There is no exaggeration in the statement. The scope of biochemistry is as vast as life itself. Every aspect of life, birth, growth, reproduction, ageing and death involves biochemistry. For that matter every movement of life is packed with hundreds of biochemical reactions. Biochemistry is the most rapidly developing and most innovative subject in medical and dental sciences.





(Quick energy supplier)

Carbon + Hydrogen + Oxygen Found in abundance in plant kingdom in the form of cellulose and starch besides this also found in animal kingdom in the form of glucose and glycogen.



Carbohydrates are neutral compounds made up of carbon, hydrogen and oxygen. H and O being in the same proportion as in water, the general formula is C n (H 2 O) n . But there are many exceptions, e.g. rhaminose (C 6 H 12 O 5 ) is a carbohydrate in which H and O are present in different proportion. Certain other compounds such as formaldehyde (HCHO) acetic acid (CH 3 COOH), lactic acid (CH 3 CHOCOOH) etc. which have got the same empirical formula but are not carbohydrates. Thus, chemically carbohydrates can be defined as the aldehyde and ketone derivative of higher polyhydric alcohol or polyhydroxy aldehydes or ketones or the compounds which produce them on hydrolysis.

Biomedical Importance

  • 1. Carbohydrates are the main source of energy.

  • 2. They are constituents of compound lipids and conjugated proteins.

  • 3. Degradation products of carbohydrates act as promoters or catalyst.

  • 4. Certain carbohydrate derivatives are used as drugs like cardiac glycosides / antibiotics.

  • 5. Degradation products are utilized for synthesis of other substances such as fatty acid, cholesterol, amino acids, etc.


Biochemistry for Dental Students

  • 7. Ribose is a constituent of nucleic acid (DNA, RNA).

  • 8. Ribose, i.e. pentose sugar also constituents certain coenzyme, e.g. FAD, NAD, coenzyme A, etc.

  • 9. Glucose is chief physiological sugar present in blood, i.e. about 0.1%.

4 Biochemistry for Dental Students 7. Ribose is a constituent of nucleic acid (DNA, RNA). 8.

Fig. 1.1: Classification of carbohydrates

Carbohydrates are classified into three classes—

I. Monosaccharides II. Oligosaccharides III. Polysaccharides (Fig. 1.1).

Carbohydrates (Quick energy supplier)


I. Monosaccharides

Simplest class of carbohydrates which cannot be further hydrolysed. These are further classified

into two groups. On the basis of their functional group they are classified as oldoses and Aldoses

  • a. Aldoses—When the functional group is an aldehyde CH-O in a monosaccharide.

  • b. Ketoses—In ketoses the functional group is a keto group C=O.

The number of carbon atoms in the monosaccharides are given in the Table 1.1.

Table 1.1: Monosaccharides and their number of carbon atoms

Sr. No.


No. of carbon atoms



  • 1. Triose



Dehydroxy acetone p

  • 2. Tetrose




  • 3 Pentose




  • 4 Hexoses




  • 5 Heptoses




So, it can be remembered that glucose is a aldohexose and fructose is a ketohexose.

General Properties of Monosaccharides

  • 1. Colourless, crystalline compound, having sweet taste, soluble in water, insoluble in benzene and ether, sparingly soluble in alcohol.

  • 2. Optical rotation—When a beam of polarised light is passed through a solution containing assymetric carbon compound then this light is rotated clockwise or to right side to be dextrorotatory represented by ‘d’ or (+) and is rotated anticlockwise or left then said to be levoratory represented by ‘l’ or (–). The mixture containing d l isomers in equal proportion is called as recemic mixture. It does not exhibit any optical activity since both d and l activities cancel each other. Freshly made solution of α glucose has specific rotation of 112°. When solution is made to stand the value falls and after 24 hours and stabilizes to 52.5°. The initial optical rotation shown by sugar gradually changes until a fixed rotation characteristic of sugar is reached.

  • 3. Sugars exist both in straight chain form and ring form. Six membered rings are called as pyranose. Five membered rings are called as furanose.


Biochemistry for Dental Students

6 Biochemistry for Dental Students Fig. 1.2: Mutarotation of glucose representing α and β anomers MUTAROTATION

Fig. 1.2: Mutarotation of glucose representing α and β anomers


Mutarotation— Mutarotation is defined as the change in optical rotation representing the

interconversion of α and β forms of D glucose to an equilibrium mixture (Fig. 1.2).

α D Glucose

<===== >



D Glucose

+ 112.2°


+ 18.7°

+ 52.7°

*(Specific optical rotation).

Mutarotation of fructose—Fructose also exhibits mutarotation. It has a specific optical rotation of -92° at equilibrium. The conversion of dextroratatory sucrose to levoratatory fructose can be explained in inversion.


If two monosaccharides differ from each other in their configuration around a single specific carbon (other than anomeric) atom, they are referred to as epimers to each other. For example— glucose and galactose are epimers (C 4 epimers), glucose and mannose are (C 2 epimers).

6 Biochemistry for Dental Students Fig. 1.2: Mutarotation of glucose representing α and β anomers MUTAROTATION

Fig. 1.3: Structures of epimers (glucose and galactose are C 4 epimers while glucose and mannose are C 2 epimers )

Carbohydrates (Quick energy supplier)



The α and β forms of D glucose are known as anomers, they differ from each other in the configuration only around C 1 known as anomeric carbon (hemiacetal carbon). In case of β anomer, the OH group held by anomeric carbon is on the opposite side of the group CH 2 OH of sugar ring and vice versa with the α anomer (Fig. 1.2).

Tautomerization or Enolization

When a hydrogen atom is shifted from one carbon atom to another to produce enediols is known as tautomerization. When glucose is kept in alkaline solution, it forms isomers D fructose and D mannose which results in the formation of a common intermediate enediol for all the three sugar. Enediols are highly reactive, hence sugars in alkaline solution are powerful reducing agents.

Reducing Properties

The sugars are classified as reducing or nonreducing. The reducing property is attributed to the free aldehyde or keto group of anomeric carbon. In lab many tests are employed to identify the reducing action of sugars. These include Benedict’s test, Fehlings test. The reduction is much more efficient in alkaline medium . The enediols or sugars reduce CuSO4 (Cu ++ ) to (Cu + ) cuprous ions which form (green <—> yellow) ppt of cuprous hydroxide or (orange<—>red) ppt of cuprous oxide depending upon concentrations of sugar. This property cannot help for specific identification of any sugar. Since, it is general reaction.

Osazone Formation

It is the reaction with hydrazine to form hydrazones which are called as osazones. Glucose + H 2 N-NH-C 6 H 5 - Phenyl glucose hydrazone These osazones are insoluble and crystallize in beautiful and characterstic form of different sugars. As it is evident from the reaction, the first two carbon (C 1 and C 2 ) are involved in osazone formation. The sugars that differ in their configuration on these two carbons give the same types of osazomes, since the difference is marked by reaction with phenyl hydrazine. Thus, glucose, fructose and mannose give same type of osazone crystal. Glucose, fructose and mannose have identical osazone crystals arranged as bundle of hay. (Broom stick) needle like Lactose forms cotton wool like crystals puffy ball like crystals. Maltose and galactose form sunflower platelet like structure.


Biochemistry for Dental Students



Glycosides are formed when the hemiacetal or hemiketal hydroxyl group (of anomeric carbon) of a carbohydrate reacts with a hydroxyl group of another carbohydrate. The bond so formed is known as glycosidic bond. The monosaccharides are held together by glycosidic bonds to result in di-, oligo- or polysaccharides. It should be noted that the reducing property of aldehyde and keto group is lost, when these groups participate in glycosidic bond formation. However, many di-and polysaccharides are reducing due to presence of other potential aldehyde or keto groups.

Naming of Glycosidic Bond

The nomenclature of glycosidic bonds is based on the linkages between carbon atoms and the status of the anomeric carbon (α or β). For instance, lactose which is formed by a bond between C 1 of β galactose and C 4 of glucose is named as β (1 – 4) glycosidic bond.

Dehydration—When monosaccharides are treated with concentrated acids, for example sulphuric acid, hydrochloric acid, etc. there occurs dehydration, thus pentoses give furfurals, and hecoses give hydroxy methyl furfurel. These furfurals can condense with phenolic compounds like α nepthol. This is the chemical base for Molisch test, which is a group test for carbohydrates.

Selivanoff’s Test

This test is specific for fructose. Resorcinol dissolved in conc HCl is added to sugar then pink colour is formed due to reaction of furfural with reasorinol.

II Oligosachharides

These type of carbohydrates are composed of 2-10 monosachharide molecules which can be obtained on hydrolysis.

The important oligosaccharides are classified as (shown in Table 1.2):

• Disaccharides Trisaccharides Tetrasaccharides Pentasaccharides. Depending on number of monosaccharide units. Among the oligosaccharides disaccharides are most common. As the name suggests, a disaccharide unit consists of two monosaccharide units (similar or dis similar) which are held together by glycoside bond. Diasaccharides are of two types—

Carbohydrates (Quick energy supplier)


  • 1. Reducing.

  • 2. Non-reducing.

Disaccharide units produce two molecules of monosaccharide units on hydrolysis. The most common disaccharides are— Lactose — Glucose + Galactose β [ 1 – 4 ] Glycosidic bond Maltose — Glucose + Glucose α [ 1 – 4 ] Glycosidic bond Sucrose — Glucose + Fructose [α 1 - β 2 ] Glycosidic bond

Table 1.2: Oligosaccharides and their monosaccharide molecules

Sr. No.


No. of monosaccharides














Lactose sucrose maltose Raffinose Stachyose Verbascose


Surcose is sugar of commerce. Its source is cane sugar. It is dextrorotatory. Hydrolysis of it by dilute acid or enzyme invertase or sucrase produce 1 molecule each of glucose and fructose which results in change in optical rotation from positive to negative because fructose is more levorotatory than D glucose.

Sucrase Sucrose + H 2 O ————Glucose + Fructose

Because of this sucrose is called as invert sugar. Honey contains a large proportion of sucrose. Sucrose is not a reducing sugar because the reducing groups of glucose and fructose are involved in glycosidic bond formation. So, it can not form osazones.


Lactose is formed by mammary glands and occurs to the extent of about 5% in milk. Therefore, it is most commonly known as milk sugar. Lactose of milk is the most important carbohydrate in the nutrition of young mammals. It is hydrolsed by enzyme lactase in to glucose and galactose. It may also be present in the urine during pregnancy. It is a reducing sugar. Souring of milk take place when lactose is converted to lactic acid. It gives osazone crystals [cotton wool shaped].


Maltose is also called as malt sugar. Maltose is composed of two glucose units and is formed by hydrolytic action of enzyme amylase or diastase on starch It is a reducing sugar. In it the glucose units are held together by α (1 – 4) linkage. It gives osazone crystals [sunflower shaped].


Biochemistry for Dental Students


It is formed during hydrolysis of certain polysaccharide also resembles maltose except that it has one α-1, 6 glycosidic linkage.


Polysaccharides consist of repeated units of monosaccharides or their derivative held together

by glycosidic linkages. They are primarily concerned with two important functions. Structural and storage of energy. Polysaccharides are of two types—

  • A. Homopolysaccharides.

  • B. Heteropolysaccharides.


When polysaccharides are composed of same types of repeated units of surgars or their derivatives they are refered to as, homopolysaccharides.


Starch is the carbohydrate reserve of plants which is the most important dietary source for higher animals, including man. High content of starch is found in cereals, roots, tubers, vegetables, etc. Starch is a homopolymer composed of D-glucose units held by α-glycosidic bonds. It is known as glucosan or glucan . Strach consists of two polysaccharide components-water soluble amylose (15-20%) and a water insoluble amylopectin (80-85%). Chemically, amylose is a unbranched chain with 200- 1,000 D-glucose units held by α (14) glycosidic linkages. Amylopectin, on the other hand, is a branched chain with α (16) glycosidic bonds at the branching points and α (14) linkages everywhere else. Amylopectin molecule containing a few thousand glucose units looks like a branched tree (20-30) glucose units per branch) (Fig. 1.4). Starches are hydrolysed by amylase (pancreatic or salivary) to liberate dextrins and finally maltose and glucose units. Amylase acts specifically on α (14) glycosidic bonds.


Dextrins are the breakdown products of starch by the enzyme amylase or dilute acids. Starch is sequentially hydrolysed to different dextrins and, finally, to maltose and glucose. The various intermediates (indentified by iodine colouration) are starch (blue), amylodextrin (violet), erythrodextrin (red) and achrodextrin. (no colour).

Carbohydrates (Quick energy supplier)


Carbohydrates (Quick energy supplier) 11 Fig. 1.4: Structures of amylose and amylopectin Inulin Inulin is a

Fig. 1.4: Structures of amylose and amylopectin


Inulin is a polymer of fructose, i.e fructosan. It occurs in dahlia bulbs, garlic, onion, etc. It is a low molecular weight (around5,000) polysaccharide easily soluble in water. Inulin is not utilized by the body. It is used for assessing kidney function through measurement of glomerular filtration rate (GFR).


Glycogen is the carbohydrate reserve in animals, hence often referred to as animal starch. It is present in high concentration in liver, followed by muscle, brain, etc. glycogen is also found in plants that do not possess chlorophyll (e.g. yeast, fungi). The structure of glycogen is similar to that of amylopectin with more number of branches. Glucose is the repeating unit in glycogen joined together by α (14) glycosidic bonds, and α (16) glycosidic bonds at branching points. The molecular weight (up to 25,000) vary in glycogen, depending on the source from which the glycogen is obtained (Fig. 1.5).


Cellulose occurs exclusively in plants and it is the most abundant organic substance in plant kingdom. It is a predominant consitituent of plant cell wall. Cellulose is totally absent in animal body.


Biochemistry for Dental Students

12 Biochemistry for Dental Students Fig. 1.5A: Showing general structure of amylose Fig. 1.5B: Showing general

Fig. 1.5A: Showing general structure of amylose

12 Biochemistry for Dental Students Fig. 1.5A: Showing general structure of amylose Fig. 1.5B: Showing general

Fig. 1.5B: Showing general structure of amylopectin which resembles with structure of glycogen

Cellulose is composed of β-D-glucose units linked by β (1 4) glycosidic bonds. Cellulose cannot be digested by mammals—including man due to lack of the enzyme that cleaves β-glycosidic bonds (β amylase breaks β bonds only). Certain ruminants and herbivorous animals contain microorganisms in the gut which produce enzymes that can cleave β-glycosidic bonds. Hydrolysis of cellulose yields a disaccharide cellobiose, followed by β-D-glucose. Cellulose, though not digested, has great importance in human nutrition. It is a major constituent of fiber, the non-digestable carbohydrate. The functions of dietary fiber include decreasing the absorption of glucose and cholesterol from the intestine, besides increasing the bulk of feces.


Chitin is composed of N-acetyl D-glucosamine units held together by β (14) glycosidic bonds. It is a structural polysaccharide found in the exoskeleton of some invertebrates, e.g. insects, crustaceans.


When the polysaccharides are composed of different types of sugars or their derivatives, they are referred to as heteropolysaccharides or heteroglycans.


These are heteroglycans made up of repeating units of sugar derivatives, namely amino-sugars and more commonly known as glycosaminoglycans (GAG) . Acetylated amino groups, besides

Carbohydrates (Quick energy supplier)


Carbohydrates (Quick energy supplier) 13 Fig. 1.6: Digrammatic representation of proteoglycan complex sulfate and carboxyl groups

Fig. 1.6: Digrammatic representation of proteoglycan complex

sulfate and carboxyl groups are generally present in GAG structure. The presence of sulfate and carboxyl groups contributes to acidity of the molecules, making them acid mucopolysaccharides. Some of the mucopolysaccharides are found in combination with proteins to form mucoproteins or mucoids or proteoglycans. Mucoproteins may contain up to 95% carbohydrate and 5% protein. Mucopolysaccharides are essential components of tissue structure. The extracellular spaces of tissue (particularly connective tissue cartilage, skin, blood vessels, tendons) consist of collagen and elastin fibers embedded in a matrix or ground substance. The ground substance is predominantly composed of GAG. A diagrammatic representation of a proteoglycan complex is depicted in Figure 1.6. The important mucopolysaccharides include hyaluronic acid, chondroitin 4-sulfate, heparin, dermatan sulfate and keratin sulfate (Fig. 1.7).

Hyaluronic Acid

Hyaluronic acid is an important GAG found in the ground substance of synovial fluid of joints and vitreous humor of eyes. It is also present as a ground substance in connective tissues and forms a gel around the ovum. Hyaluronic acid serves as a lubricant and shock absorbent in joints. Hyaluronic acid is composed of alternate units of D-glucuronic acid and N-acetyl D- glucosamine. These two molecules form disaccharide units held together by β (13) glycosidic bond. Hyaluronic acid contains about 250-25,000 disaccharide units (held by β 14 bonds) with a molecular weight up to 4 million.


Biochemistry for Dental Students

14 Biochemistry for Dental Students Fig. 1.7: Figure of structure of common glycosaminoglycans the disaccharides as

Fig. 1.7: Figure of structure of common glycosaminoglycans the disaccharides as repeating units

Hyaluronidase is an enzyme that breaks (β 14 linkages) hyaluronic acid and other GAG. This enzyme is present in high concentration in testes, seminal fluid, and in certain snake and insect venoms. Hyaluronidase of semen is assigned an important role in fertilization as this enzyme

Carbohydrates (Quick energy supplier)


clears the gel (hyaluronic acid) around the ovum allowing a better penetration of sperm into the ovum. Hyaluronidase of bacteria helps their invasion into the animal tissues.

Chondroitin Sulfates

Chondroitin 4-sulfate (Greek: chondroscartilage) is a major constituent of various mammalian tissues (bone, cartilage, tendons, heart, valves, skin, cornea etc.) Structurally, it is comparable with hyaluronic acid. Chondroitin 4-sulfate consists or repeating disaccharide units composed of D-glucuronic acid and N-acetyl D-galactosamine 4-sulfate.

Chondroitin 6-sulfate is also present in many tissues. As evident from the name, the sulfate group is found on C 6 instead of C 4 .


Heparin is an anticoagulant (prevents blood clotting) that occurs in blood, lung, liver, kidney, spleen etc. Heparin helps in the release of the enzyme lipoprotein lipase which causes clearing the turbidity of lipemic plasma. Heparin is composed of alternating units of N-sulfo D-glucosamine 6-sulfate and glucuronate


Dermatan Sulfate

The name dermatan sulfate is derived from the fact that this compound mostly occurs in the skin. It is structurally related to chondroitin 4-sulfate. The only difference is that there is an inversion in the configuration around C 5 of D-glucuronic acid to form L-iduronic acid.

Keratan sulfate

It is a heterogeneous GAG with a variable sulfate content besides small amounts of mannose, fructose, sialic acid, etc. Kertan sulfate essentially consists of alternating units of D-galactosamine and N-acetylglucosamine 6-sulfate.


1. Carbohydrates are the aldehyde and Ketone derivative of higher polyhydric alcohol. The term sugar is applied to carbohydrate soluble in water and sweet to taste. They are the main source of energy and play an important role in various other function. 2. Carbohydrates are classified into three groups—Monosaccharide, disaccharides and polysaccharides.


Biochemistry for Dental Students

Monosaccharide are further divided on the basis of functional groups as oldeses and ketoses and on the basis of number of carbon atoms they are classified as trioses, tetroses, pentoses, hexoses and heptoses.

  • 3. Glyceraldehyde is the simplest carbohydrate. If two monosaccharides differ in their structure around a single carbon atom, they are known as epimers glucose and galactose are C 4 epimers.

  • 4. Glucose is most predominant as far as the occurrence of monosaccharides in nature is concerned. It exists in α and β anomeric forms. The interconversion of α and β forms is called as mutarotation.

  • 5. Monosaccharides show various chemical properties including oxidation, reduction dehydration, osazone formation, formation of esters and glycosideic linkages.

  • 6. Lactose, maltose and Sucrose. These three diasaccharides are the most common oligosaccharides, maltose and lactose are reducing diasaccharides but sucrose is nonreducing sugar. It shows inversion.

  • 7. The polymers of monosaccharides are called as polysaccharides, the monosaccharides are held together by glycosides linkage.

  • 8. Polysaccharides are classified as homopolysaccharides and heteropolysaccharides.

  • 9. Homopolysaccharides are composed of a single monosaccharides (example–starch, glycogen).

10. Heteropolysaccharides contain mixture of few monosaccharides, e.g. mucopolysaccharides.



(The concentrated storage form of energy)


Lipids constitute very important group of organic substances in plants and animals. Chemically they are various types of esters of fatty acids with different alcohols.


Insoluble in water, readily soluble in ether, chloroform, benzene, carbon tetrachloride. They are good solvents for fats and fatty acids. These are tasteless, odourless, colourless and neutral in reaction.

Biomedical Importance

  • 1. Lipids are important dietary constituent and acts as fuel in the body.

  • 2. To some respect lipids are superior to carbohydrates as a raw material for combustion, i.e. when 1 gram of fat or lipid is burnt then 9.7 calories of energy or heat is produced. It yields 9.7 cal/gm of energy while carbohydrates yield 4 cal/ gm.

  • 3. Lipids can be stored in the body in almost unlimited amount as compared to carbohydrates.

  • 4. They exert an insulating effect in the body.

  • 5. Lipids present around internal organs, e.g. lipids protect the organ from mechanical shock.

  • 6. Break down products such as acetyl CoA are used for building complex biological active materials like cholesterol which in turn can be utilized for synthesis of certain harmones, e.g. progesteron.

  • 7. Lipids supply fatty acids essential in the diet for normal health and growth. (Those which cannot be synthesized in the body).

  • 8. The nervous system is particularly rich in phospholipids. Non-polar lipids acts as electrical insulators allowing rapid propogation of depolarization waves along myelinated nerves.

  • 9. Fats are also components of vitamins like A, D, E and K (nepthoquinone).

10. Lipoprotein and phospholipids are important constituents of many natural membranes such as cell walls and cell organelles like mitochondrion.


Biochemistry for Dental Students

11. Lipoproteins serve as carriers of triglycerides, cholesterol and phospholipid in the body. Knowledge of lipid is important in understanding many current biomedical areas of interest e.g. obesity, atherosclerosis and role of various polyunsaturated fatty acids in nutritional health.

Classification of Lipids

Lipids are classified into three classes (Fig. 2.1)

  • 1. Simple lipids.

  • 2. Compound lipids.

  • 3. Derived lipids.

    • I. Simple Lipids

Simple lipids are esters of fatty acids with alcohols.These are mainly of two types—

  • A. Fats and oils or neural fats.

  • B. Waxes.

  • A. Fats—Triacylglycerol or triglycerides (Fig. 2.2)

  • A. Fats and oils: These are the esters of fatty acids with glycerol. Triacylglycerol are the most

abundant group of lipids which acts as fuel reserve in animals and human.

18 Biochemistry for Dental Students 11. Lipoproteins serve as carriers of triglycerides, cholesterol and phospholipid in

Fig. 2.1: Classification of lipids

Lipids (The concentrated storage form of energy)


Lipids (The concentrated storage form of energy) 19 Fig. 2.2: Structure of triacylglycerol Triacyl glycerols are

Fig. 2.2: Structure of triacylglycerol

Triacyl glycerols are of two types—simple triacylglycerol and mixed triacylglycerol.

Simple Triacylglycerol

These type of triacylglycerol contain the same type of fatty acids at the three carbon atoms.

Mixed Triacylglycerol

These are more common. These contain two or more types of different residues. In general fatty acids attached to C 1 is saturated while FA attached to C 2 is unsaturated while in case of C 3 that can be either.

Properties of Triacylglycerols

A few important properties of triacylglycerol have been discussed below.

  • 1. Hydrolysis: In triglycerides there occurs step wise hydrolysis to form fatty acids and glycerol.

This occurs by lipases. It is important for digestion of fat in gastrointestinal tract and mobilization

of fat from adipose tissues.

  • 2. Saponification: The hydrolysis of triacylglycerols to produce glycerol and soaps is known as


Triglycerides + Alkali

> Glycerol + Soap


  • 3. Rancidity: It is the term used for deterioration of fats and oil resulting in unpleasant taste and smell. Fats containing unsaturated fatty acids are more susceptible to rancidity.

When fats and oils are exposed to air moisture, light or bacteria, rancidity occurs. Rancidity is of two types—


Hydrolytic Oxidative rancidity rancidity


Biochemistry for Dental Students

Hydrolytic Rancidity

It occurs due to hydrolysis (partial) of triglycerides in presence of bacterial enzymes.

Oxidative Rancidity

It occurs due to oxidation of unsaturated fatty acids to form dicarboxylic acid, aldehydes ketones, etc. which are very unpleasant products. The oils and fats after rancidity are called as rancid oils and rancid fats which are very unsuitable for human consumption.


The substances which prevent the occurance of oxidative rancidity are called as antioxidant. These are tocopherol (Vit. E), hydroquinone, α nepthol. These are added in the commertial preparation of fats and oils.

Lipid peroxidation

By oxidation of lipids in living cells, there occurs formation of peroxides and free radicals which cause inflammatory diseases, aging, cancer, atherosclerosis and therefore, we must take Vit. E in diet, although the cells themselves have Vit. E, urate, superoxide dismutase to fight against peroxidation.

B. Waxes

These are the esters of fatty acids usually long chains of fatty acids with alcohol other than glycerol. The alcohol may be aliphatic or alicyclic. Cetyl alcohol is most common in waxes.


Compound lipids are esters of fatty acids with alcohol containing an additional group such as phosphate, nitrogenous base, carbohydrates, proteins, etc.

  • I. Phospholipids: These are the compound lipids which contain phosphoric acid complexed with lipids. There are of two types of phospholipids glycerophosphatides or phosphoglycerides and sphingomyelins (containing sphingosine as alcohol). Glycerophosphatides: These are the major lipids occurring in biological membrane. They contain glycerol 3 phosphate esterified with fatty acids at C 1 and C 2 , C 1 contain saturated fatty acid while C 2 contain unsaturated fatty acid.

Lipids (The concentrated storage form of energy)


I. Phosphatidic Acid

This is the simplest phospholipids or we can say that it is the intermediary product between triglycerides and phospholipids. There occurs addition of nitrogen bases or other groups to form the compounds like lecithin cephalin and plasmalogens.

  • A. Lecithins—Also called as phosphalidyl cholin containing phospholidic acid with choline as base. These are also found in liver and sperm.

  • B. Cephalins—Also called phospholidyl ethanol amine as it contains ethanolamine as base these are also found in milk and these are identical with thrombokinase which initiates the blood clothing.

  • C. Phasmalogens—When a fatty acid is attached by ether linkage at C 1 of glycerol in glycerolphosphatide there occurs formation of plasmalogens. They are chemically phosphatidal ethnolamine. These are also found in liver and muscles.

II. Sphingomyelin

Instead of glycerol, these contain sphingosine as alcohol they do not contain glycerol at all. These are called as sphingomyelins as they are abundant in the myelin sheaths of nerve fibres.

  • 2. Nonphosphorylated Lipids

    • A. Glycolipids: Also called as cerebrosides found in white matter of brain composed of shingosine fatty acids and brain sugar, i.e. galactose and sphingosine attached with fatty acid is called. as ceramide, galacto cerebrosides and glucocerebroside are most important glycolipids, gangliosides found in ganglion of brain are derived from these cerebrosides.

    • b. Lipoproteins or proteolipids: These are the molecular complexes of lipids with proteins. They are the transport vehicles for lipids in circulation. There are five types of lipoproteins, they are chylomicrons, very low density lipoporteins, low density lipo- proteins (LDL), high density lipoproteins (HDL) and free fatty acid albumin complexes.

  • 3. Steroids

  • Steroids are the compounds containing a cyclic steriod nucleus or 4 ring fused structure (Fig. 2.3). The name of the nucleus is cyclopanteno perhydro phenanthrene it contains phenanthrene nucleus to which cyclopanteno ring is attached. There are several steroids found in biological system. These include cholesterol, bile acids, the structure of steroid neccleus is given in Figure 2.3, with two examples, cholesterol and ergosterol, vit D, sex hormones, adrenocortical hormones.


    Biochemistry for Dental Students


    Cholesteral is exclusively found in animals and is most abundant animal sterol. Sterol means solid alcohol. It is widely distributed in all cells and is major component of cell membranes cholesterol (Greek : chole bile) was first isolated from bile so, cholesterol means solid alcohol from bile.

    22 Biochemistry for Dental Students Cholesterol Cholesteral is exclusively found in animals and is most abundant

    Fig. 2.3: Structures of steroids

    Cholesterol contains cyclopanteno perhydrophenen thrine with hydroxyl group.

    Functions of Cholesterol– Its function is to act as insulating cover in the nervous tissues. Cholesterol performs several biochemical functions which include synthesis of bile acids, hormones (sex and cortical) and Vitamine D.

    Ergosterol— Found in plants and performs the function to produce ergocalciferol which is a compound containing vit D activity.


    Derived lipids are the derivatives obtained during hydrolysis of simple and compound lipids. They are fatty acids and glycerol.

    Lipids (The concentrated storage form of energy)


    • 1. Glycerol: It is commonly called as glycerin, simplest trihydroxy alcohol.

    Lipids (The concentrated storage form of energy) 23 1. Glycerol: It is commonly called as glycerin,

    It is colourless oily fluid with a sweetish test.


    • 1. Endogenous.

    • 2. Exogenous.

    Endogenous sourceIt is obtained by lipolysis of fats in adipose tissues.

    Exogenous sourceApproximately 22% of glycerol is directly absorbed to portal blood from gut. It has definite nutritive value. It can be converted to glucose and glycogen by gluconeogenesis.

    Biomedical Importance

    In Medicine

    • 1. Nitroglycerine is used as vasodilator.

    • 2. Glycerol is given orally as well as intravenously in cerebrovascular disease.

    • 3. Intra-venous drip of mannitol is given to patients to reduce cerebral oedema.

    • 2. Fatty acids: Fatty acids are carboxylic acids with hydrocarbon side chain. They are the simplest

    form of lipid. Fatty acids are divided into two classes—saturated and unsaturated. Saturated fatty acids contain only single bond, e.g. acetic acid, butyric acid—it is butter fat, palmitic acid, steroic acid (selected example of saturated fatty acids are given in the Table 2.1).

    Unsaturated fatty acids contain one or more double bonds, e.g. oleic acid.

    Unsaturated fats are more common in living organisms than saturated fats. Fatty acids containing more than one double bond are called as polyunsaturated fatty acids, i.e. PUFA. For example

    Linoleic acid—Found in peanut oil, soyabean oil, cotton seed oil, egg yolk, etc.

    Linolenic acid—Found in soyabean oil linseed oil, cod liver oil, etc.

    Arachidonic acid—Found in peanut oil and liver fat.


    Biochemistry for Dental Students

    These 3 polyunsaturated fatty acids are called as essential fatty acids. EFA as these are Not synthesized in body, and therefore must be supplied in the diet. (Essential fatty acids with other unsatarated fatty acids are given in the Table 2.1).

    Table 2.1: Selected examples of biochemically important fatty acids

    Common name

    Systematic name



    I. Saturated fatty acids

    Acetic acid

    Ethanoic acid


    Propionic acid

    n-Propanoic acid


    Butyric acid

    n-Butanoic acid


    Valeric acid

    n-Pentanoic acid


    Caproic acid

    n-Hexanoic acid


    Caprylic acid

    n-Octanoic acid


    Capric acid

    n-Decanoic acid


    Lauric acid

    n-Dodecanoic acid


    Myristic acid

    n-Tetradecanoic acid


    Palmitic acid

    n-Hexadecanoic acid


    Stearic acid

    n-Octadecanoic acid


    Arachidic acid

    n-Cicosanoic acid


    Behenic acid

    n-Docosanoic acid


    Lignoceric acid

    n-Tetracosanoic acid


    II. Unsaturated fatty acids

    Palmitoleic acid

    cis-9-Hexadecenoic acid


    Oleic acid

    cis-9-Octadecenoic acid


    Linoleic acid***

    cis, cis-9 12-Octadecadienoic acid


    Linolenic acid***

    All cis-9, 12,


    15-Octadecatrienoic acid


    Arachidonic acid***

    All ciAll cis-5,8,11,14-


    Eicosatertraenoic acid


    CH 3 COOH CH 3 CH 2 COOH

    CH 3 (CH 2 ) 2 COOH CH 3 (CH 2 ) 3 COOH CH 3 (CH 2 ) 4 COOH CH 3 (CH 2 ) 6 COOH CH 3 (CH 2 ) 8 COOH

    CH 3 (CH 2 ) 10


    CH 3 (CH 2 ) 12


    CH 3 (CH 2 ) 14


    CH 3 (CH 2 ) 16


    CH 3 (CH 2 ) 18


    CH 3 (CH 2 ) 20


    CH 3 (CH 2 ) 22


    CH 3 (CH 2 ) 5 CH=CH(CH 2 ) 7 COOH CH 3 (CH 2 ) 7 CH=CH(CH 2 ) 7 COOH CH 3 (CH 2 ) 4 CH=CHCH 2 CH=CH (CH 2 ) 7 COOH CH 3 (CH 2 )CH=CHCH 2 CH= CHCH 2 CH=CH(CH 2 ) 7 COOH CH 3 (CH 2 ) 4 CH=CHCH 2 CH=CH CH 2 CH=CHCH 2 CH=CH(CH 2 ) s COOH

    Total number of carbon atoms, followed by number of double bonds and the first carbon position of the double bond(s). *** Essential acids synthesized in the body.



    • 1. They are structural elements of tissues gonads and mitochondrial membrane.

    • 2. Involved in synthesis of prostaglondins and leukotrienes.

    • 3. Serum level of cholesterol is lowered by fats with high content of PUFA.

    • 4. They play role in vision and enhance the electrical response of the photo receptors of illumination.

    Lipids (The concentrated storage form of energy)


    Deficiency Manifestations or Symptoms

    • 1. Stopage or slow growth rate.

    • 2. Skin lessions, hyperkeratosis eczema like dermatitis. One seterik is showing abbrivation which means total no. of carbon atoms, followed by double bonds and the first carbown position of double bonds in case of unsaturated fatty acid. I am putting sign there and three asteiks are representing essential futty acids in the table.

    • 3. Skin becomes abnormally permeable to water i.e. increased loss of water increases BMR– Basal Metabolic rate.

    • 4. Abnormalities in pregnancy.

    • 5. Fatty liver accompanied by increased rates of fatty acids synthesis.

    • 6. Lessened resistance to stress.

    • 7. Kidney damage.

    • 8. Degenerative changes in arterial wall.

    • 1. Lipids are chief concentrated storage form of body.

    • 2. Lipids are organic substances selectively insoluble in water and soluble in organic solvants.

    • 3. They are classified as simple lipids (facts and waxes) compound lipids (phospholipids and nonphospho lipids ) and derived lipids (fatty acids glycerol and ketone bodies).

    • 4. Simple fats are also called as triacylglycerol. These are the esters of fatty acids with glycerol primarily they are the major fuel reserve of animals.

    • 5. Phospholipids are the compound lipids containing phosphoric acid while nonphospholipids do not contain phosphoric acid, e.g. glycolipids.

    • 6. Cerebrosides are simplest form of glycolipids which occur in the membranes of nervous tissues.

    • 7. Steroids contain cyclicring known as cyclopantenoperhydrophenenthrene. Biologically important steroids are cholesterol, bile acids, vit D, sex hormones, etc.

    • 8. The derived lipids are fatty acids glycerol and ketone bodies.

    • 9. Fatty acids are divided into two groups saturated fatty acids and unsaturated fatty acids. The poly unsaturated fatty acids namely linoleic acid, linolenic acid and arachidonic acid which need to be supplied in the diet.



    (The structural and functional basis of life)

    • I. Definition of Proteins

    This term is derived from a Greek word “PROTEIUS” means primary or holding first place or pre-eminent because they are the most important biological substances. The proteins can be defined as the nitrogenous macromolecules composed of many amino acids.

    II. Biomedical or Clinical Importance

    • 1. Proteins are main structural component of cytoskeleton.

    • 2. Proteins are the sole source to replace nitrogen of body (since 15 g of nitrogen is lost everyday by a well fed normal adult chiefly as urinary urea). Therefore proteins are chief dietary sources or constituent for supply of nitrogen as well as phosphorus.

    • 3. All enzymes which are called biological catalysts are proteinous in nature.

    • 4. Proteins called as immunoglobulins serve as first line of defence against bacterial and viral infection.

    • 5. Several hormone are proteinous in nature. These regulate many aspects of cell functions e.g. estrogen, progesterone, etc.

    • 6. Structural protein provide mechanical support and some proteins are called as contractile proteins, e.g. actin and myosine provide movements to muscles and therefore to body.

    • 7. Some proteins are present in cell membrane cytoplasm and nucleus which are called as receptors. They bind specific substances such as vitamins, harmones, etc. and mediate their cellular action.

    • 8. The transport protein carry out the function of transporting specific substances either across the membrane or body fluids.

    • 9. Storage proteins bind with specific substances and store them, e.g. iron is stored as ferritin.

    10. Few Proteins are constituents of respiratory pigments and occur in election transport chain

    or respiratory chain, e.g. cytochromes, Hb, myoglobins 11. Under certain conditions proteins can be catabolized to supply energy when lipids carbohydrates stores of body are exhausted.

    Proteins (The structural and functional basis of life)


    12. Proteins by means of exerting osmotic pressure help in maintenance of electrolyte and water balance in body.


    Proteins are essential constituents of protoplasm. They differ from carbohydrates and lipids by always containing nitrogen and sometimes sulphur and phosphorus. The elementary composition of protein is as follows :

    Carbon - 54%

    Hydrogn -


    Nitrogen -


    Oxygen - 22% Some may contain sulphur - 1% while others phosphorus - 0.6%.

    Classification of Proteins

    The proteins are classified on three basis.

    • I. Classification based on nutritional basis.

    II. Classification based on chemical nature.

    III. Classifications based on functions.

    Classification Based on Nutritional Basis

    Class I Proteins

    Protein that contain all the essential amino acids in addition to nonessential amino acids are called as Class I proteins. All animal proteins, e.g. meat, fish, milk, egg, etc. are class I or type I proteins. Proteins in which one or more amino acids are missing are called as class II proteins, e.g. All proteins of vegetable origin exception rice protein is class I protein. Supplementary Proteins: Wheat contains gliadin and glutenin. Gliadin lacks in lysine but glutenin is rich in lysine. One eats wheat as a whole and the requirement is fulfilled.

    Classification of Proteins Based on Chemical Nature (Table 3.1)

    • 1. Simple protein: They are composed of only amino acid residue.

    • 2. Conjugated proteins: Besides amino acids these proteins contain a non-proteinousmoiety called as prosthetic group or conjugating group.


    Biochemistry for Dental Students

    I SIMPLE PROTEINS: These are classified into two classes.

    • A) Globular: spherical or oval shaped, soluble in water or other solvent, easily digestible

    • B) Scleroproteins: These are fibrous proteins i.e. fiber like in shape insoluble in water and

    resistant to digestion.

    Table 3.1: Classification of proteins




    (Not Combined with Anything)


    (These remain combined with non

    • 1. Proteins


    Protamines – Sperm Proteins


    • 2. Meta proteins

    • 1. Chromoproteins – Hb, cytocrome,

    • 2. Phosphoproteins – caesinogen of

    • 3. Proteoses




    Histones – Thymus histone, Hb.

    Albumin – Serum albumin, oval (egg) lactalbumin.

    visual purple.


    • 4. Peptones

    • 5. Polypeptide

    • 6. Dipeptide

    Globulin – Serum globulin vitulline


    Prolamines – Gliadin (wheat) zein

    • 3. Nucleoproteins – Nucleic acid.

    • 7. Amino acids



    • 4. Glycoproteins – Mucin (saliva) hexosamine.

    • 5. Lipoproteins – Phospholipids, egg,

    • 6. Metalloproteins – Enzymes, e.g.


    Glutelins – Wheat



    carbonic, anhydrase.




    2. Elastic

    3. Keratin


    tissue e.g.



    Tendons and

    horns, etc.





    • 1. Nucleoproteins: Protein group with nucleic acids (DNA and RNA).

    • 2. Glyco proteins: Protein is found in combination with carbohydrates which is less than 4% and if carbohydrate content is more than 4% then called as muco protein, e.g. mucin, glucosamine.

    • 3. Lipoprotein: Serum lipoprotein, membrane lipoprotein.

    • 4. Phosphoprotein: Phosphoric acid, casinogen milk.

    • 5. Chromoprotein: Coloured natured protein, e.g. Hb, cytocromes.

    • 6. Metalloprotein: Protein group with metal ion e.g. Fe, Co, Zn, e.g. carbonic anhydrase, ceruloplasmin.

    Proteins (The structural and functional basis of life)


    Proteins (The structural and functional basis of life) 29 CLASSIFICATION BASED ON FUNCTIONS S = Structural



    = Structural proteins, e.g. keratin of hair, nail.


    = Enzyme proteins – Hexokinase, pepsinogen.


    = Transport proteins – Serum albumin, Hb.

    G = Genetic proteins – DNA, RNA.


    = Defence proteins – Serum globulins, immunoglobulins.


    = Receptors proteins – Receptors for hormone.


    = Storage proteins - Glutelins, ovalbumin.


    = Contractite proteins - Actin, myosin.

    H = Hormonal Proteins - Insulin, growth hormone.


    Structural hierarchy of proteins is comparable to a building. The amino acids can be compared to the bricks, the wall can be considered as primary structure, the twists in walls as secondary structure, a full pledged self-contained room as tertiary structure. The building with similar and dissimilar room may be considered as the quarternary structure. The structure of protein is rather complex and it can be divided into four levels of organization.

    • I. Primary Structure: The linear sequence of amino acids forming the back bone of proteins (polypeptide).

    II. Secondary Structure: The special arrangement of protein by twisting of the polypeptide chain

    III.Tertiary Structure: The three dimensional structure of a functional protein.

    IV. Quaternary Structure: Special arrangement of subunits, i.e. if a protein contains 2 or more polypeptide chains then these chains are called as sub units. So the special arrangement of these subunits is called as the quaternary structure.


    Biochemistry for Dental Students

    Primary Structure

    Primary structure of protein involves the amino acids which are the building blocks of protein they are held together by means of a covalent bond which is k/a peptide bond. These peptide bonds are very stronger in nature and can be considered as the cementing material between the brick as shown in Figure 3.1.

    30 Biochemistry for Dental Students Primary Structure Primary structure of protein involves the amino acids which

    Fig. 3.1: Formation of a peptide bond

    Formation of a peptide bond: When the amino group of an amino acid combines with the carboxyl group of another amino acid, a peptide bond is formed (as shown in the Figure 3.1). It should be noted here that depeptide will have two amino acids and one peptide bond (not two). Peptides containing more than 10 amino acids (deca peptides) are referred to as polypeptides.

    II. Secondary Structure

    The confirmation of protein by twisting or folding is called as secondary structure of protein. Two types of secondary structures are proposed (a) α helical structure (b) β pleatical structure.

    • A. α-Helix:– α-helix is the most common spiral structure of proteins. It is a stabilized by extensive hydrogen bonding. It is formed between H atom attached to peptide N and O atom attached to peptide C. The individual hydrogen bond is weak, but collectively hydrogen bonds are very strong enough to stabilize secondary structure (α-helix) of proteins. As it is shown in Figure 3.2.

    • B. Parallel and antiparallel β Sheets:– In this type of arrangement, the polypeptide chains are arranged in parallel (in some direction) or antiparallel (in opposite direction). β-pleated sheets may be formed either by interchain hydrogen bonding means the hydrogen bonding between the two different polypeptide chains or by intrachain hydrogen bonding means a single polypeptide chain folding back to itself. As given in Figure 3.3. The secondary structure of protein involves hydrogen bonding between the neighbouring

    segments of a polypeptide chains.

    Proteins (The structural and functional basis of life)


    Proteins (The structural and functional basis of life) 31 Fig.3.2: Secondary structure ( α -Helix) Fig.

    Fig.3.2: Secondary structure (α-Helix)

    Proteins (The structural and functional basis of life) 31 Fig.3.2: Secondary structure ( α -Helix) Fig.

    Fig. 3.3: A. Beta pleated sheet, B. Parallel β sheet, C. Antiparalled β sheet


    Biochemistry for Dental Students

    32 Biochemistry for Dental Students Fig. 3.4: Digrammatic representation of protein structure III Tertiary Structure The

    Fig. 3.4: Digrammatic representation of protein structure

    III Tertiary Structure

    The three dimensional arrangement of protein structure is referred to as the tertiary structure. This structure involves besides hydrogen bonding disulfide bonds. Electrostatic bonds and hydrophobic bonds. The term domain is used to represent the basic unit of protein structure (upto tertiary stage structures) (Fig. 3.4).

    IV Quarternary Structure

    Several manomer units join together to form oligomer which is a quartarnary structure of protein, e.g. Hb is tetramer and several isozyme like lactic dehydrogenase (tetramer) or creatine phosphokinase (a dimer). Disintegration of monomeric subunits results in loss of biological activity of protein (Fig. 3.4). Bonds responsible for quarternary structure of proteins: The quarternary structure of protein involves, the non-covalent bonds namely hydrogen bonds, hydrophobic interaction and ionic bonds.


    Physical Properties

    • 1. Proteins are colloidal in nature but many of them can be crystallized.

    • 2. Proteins vary in their M. weights and shapes.

    • 3. Each protein has got a particular iso-electric pH or iso-electric point at which it is precipitated. During this precipitation they do not undergo any intramolecular changes they are precipitated because the pH is not suitable for them.

    Proteins (The structural and functional basis of life)


    Group Tests of Proteins

    There are three group tests by which they are identified I. Precipitation reaction: Proteins exist in colloidal form of polar groups (-Co, NH 2 , - OH) Proteins can be precipitated by dehydration or neutralization of polar groups, several methods are used to achieve protein precipitation. i. Precipitation by salt of heavy metals – FeCl 3 . ii. Precipitation by acids – Nitric acids – Hiller’s test. iii. Precipitation by alkaloids – Sulphosalysilic acid.

    ppt= precipitation

    II. Coagulation reaction III. Colour reaction.

    Salting out

    Salting out

    Precipitation of protein by

    Salting in

    I. Precipitation Reaction

    Proteins are precipitated by following as shown in Table 3.2.

    Table 3.2: Agents that help in precipitation of protein

    Salts of heavy metals HgCl 2 , FeCl 3

    Certain acids (alkaloidal reagents) e.g. picric acid, tannic acid

    Concentrated solution of (NH 4 ) 2 SO 4 , Na 2 SO 4, NaCl

    Alcohol Acetone(dehydrating reagent) these cause denaturation of proteins and also dehydration.


    II. Coagulation Reaction

    Coagulation of protein is caused by denaturation of protein structure.


    The phenomenon of disorganization of native structure of proteins is known as denaturaiton. Denaturation results in the loss of secondary, tertiary and quarternary structure of proteins. This involves change in physical, chemical and biological properties of proteins. The physical agents for denaturation are heat, violent shaking, X-rays, etc. and chemical agents are: Acids, alkalies, salts of heavy metals, etc.

    III. Colour Reactions

    The proteins give several colour reactions which are often useful to identify the nature of amino acids present in them.


    Biochemistry for Dental Students

    • A. Biuret reaction: Biuret is a compound formed by heating urea to 180°C. When biuret is

    treated with dilute CuSO 4 in alkaline medium a purple colour is obtained. It is believed that this colour is due to formation of a copper coordinated complex. Biuret test is answered by compounds containing two or more CONH group or peptide

    bonds. The principle of Biuret test is conveniently used to detect presence of proteins in biological fluids (oxamide) CONH 2 + Biuret.

    • B. Ninhydrin Test: This test is used to detect presence of α - amino acids in a powder. It is positive for proteins, peptones, peptide including ammonia. The triketohydrantin hydrate forms a complex with amino or carboxylic group of amino acids or other primary amine developing a blue colour.

    Requirement of Protein

    Protein requirement for different section of the people is shown in Table 3.3.

    Table 3.3: Requirement of protein



    Protein Requirement in gm


    0-5 months 5 months - 1 year

    13 gm/ day 14 gm


    1-3 years


    4-6 years


    7-10 years



    11-14 years


    15-18 years


    19-24 years


    25-50 years





    11-14 years


    15-18 years


    19-24 years


    25-50 years




    Pregnant women



    First 6 months


    second 6 months



    The total volume of blood in adult is around 4-5.5 lit. Blood performs several classified functions. These include respiration, excretion, acid base balance, water balance, transport of metabolites, hormones and drugs body defense and coagulation.

    Proteins (The structural and functional basis of life)


    The name and function of plasma proteins can be listed as under Table 3.4.

    Table 3.4: Name and function of plasma protein


    Functions of plasma proteins

    Clinical significance


    • i. Osmotic pressure: Albumin because of their high concentration and low molecular weight contributes to the plasma osmotic pressure. A decrease in this pressure leads to excess fluid accumulation in tissue space causing oedema. This occurs in the patients suffering from Kwashiorkar (A protein energy malnutrition disorder) is due to a decrease in the plasma albumins.

    ii. Transport functions: Albumin is involved in the transportation of important compounds like bilirubin free fatty acids, steroid hormones, calcium and copper. Several drugs like aspirin, penicillin, etc. are also transported through circulation after binding with albumin.

    Normal value in plasma is 3.5 to 5 gm / dl. Decreased level of albumin is seen in hypoalbuminemia.

    • i. Decreased protein intake.

    ii. Cirrhosis of liver (liver is in the site

    of albumin synthesis. iii. Nephrotic syndrome due to loss of albumin in urine is called albumineria. iv. During burns albumin is lost through the unprotected skin surface.

    iii. Buffering action: Albumin act as buffers and maintain the acid base balance in the body. They are the most powerful buffer amongst the other plasma proteins, but their buffering action is negligible compared to bicarbonate buffer system.Reverse source of amino acids for tissue during nutritional deprivation of amino acids.

    Globulins antitrypsin or anti proteinase upon electrophorasis this protein occupies


    α 1






    It is serine protease inhibitor, i.e. it inhibits all the proteolytic enymes having serine in their active center, e.g. plasmin, thrombin, trypsin, chymotrypsin, elastase, etc.

    Normal level in plasma less than 0.2 gm/ dl. Antitrypsin deficiency has been associated with following disorers. Emphysema this disease is characterized by abnormal distension of lungs with air.During lung infection like pneumonia, the alveolar macrophages release elastase which destroys lung tissues. Under normal circumstances elastase is inhibited by L1. Antitrypsin but its deficiency leads to uncontrolled elastase activity causing destruction to large amount of lung tissues. Liver disease: Due to a defect in gene coding of α 1 AT mutant α 1 AT is produced which aggregate to form

    Contd ...


    Biochemistry for Dental Students

    Contd ...


    Functions of plasma proteins

    Clinical significance

    α 2


    polymers. These polymers cause liver damage and to subsequent cirrhosis.

    It inactivates all proteases. It is an important in vivo anticoagulant.

    Normal plasma concentration of α 2 macroglobulin is 0.2 to 0.3 g/dl. Its levels are elevated in nephrotic syndrome, because other proteins of low molecular weight are lost through urine.

    Haptoglobin upon electrophoresis this protein occupies the globulin frac- tion of plasma proteins.

    Some amount of Hb during hemolysis spills into plasma. This is called extracorpuscular Hb. This free Hb can easily penetrate through the filtering membrane of glomeruli of nephrons. Haptoglobin combines with this free Hb to form a haptoglobin-hemoglobin complex which cannot pass through the filtering membrane.

    Normal plasma concentration is <0.3 g/dl concentration decreases in hemolytic anemia.

    Ceruloplasmin upon electro- phoresis this protein occupies. The L2 globulin fraction of plasma proteins.

    90% copper in plasma is bound to ceru- loplasmin. It is involved in transport of copper and oxidation of Fe +++

    Transferin– These protein occupy the B globulin fraction of plasma protein upon electrophorosis

    Iron is transported in plasma after it combines with transferin.

    Normal plasma concentration. ceruloplasmin is 0.25 to 0.5 g/dl levels are decreased in Wilson’s disease. This disease is characterized by increased accumulation of copper i. In liver leading to cirrhosis ii. In basal ganglia leading to neurological symptoms and necrosis. iii. In kidney causing renal failure iv. In bone marrow causing hemolytic anemia.

    Immunoglobulin– These proteins occupy the γ globulin fraction of plasma proteins upon electro- phoresis they are of 5 different types namely IgG, IgA, IgM, IgE, IgD. Can be remembered as (GAMED) [IgG].

    It is most abundant Ig. It is the only Ig which can cross the placental barrier and transfer the mother’s immunity to foetus.IgG can bind with microbes and sensilizse them for killing by lymphocytes and macrophages a process called opsonization.

    Erythroblastosis foetalis or HDN (hemolytic disease of new born). This condition occurs when the mother is Rh-ve and the foetus is Rh+ve during the second pregnancy.

    Contd ...

    Proteins (The structural and functional basis of life)


    Contd ...


    Functions of plasma proteins

    Clinical significance





    i. These are large Ig which are very effective against invading microbes. ii. First antibodies to be produced against invading microbes. iii. Natural antibodies like ABO system antibodies are IgM in nature.

    Because of their large size they cannot cross the placenta hence the foetus though if it has an incompatible blood group antigen is protected from the natural antibodies of the mother.

    Its function is not known for certain, lust it is believed that it is involved in antigen recognition.

    These are referred to as secretory antibodies because they are present in bodily secretions like saliva, tears, sweat, secretions of GIT, nasopharynx, urogenital tract, etc.

    These antibodies are involved in allergy, hypersensitively and anaphylasis. They fix themselves to basophils and mast cells and bring about degranulation histamine which causes vasodialation and bronchoconstriction.

    Penicillin anaphylaxis; when pencillin is injected a few times IgE antibodies are produced which anchor themselves to mast cells when it is injected next time, the antigen present in it will fix themselves to the antibodies causing degranulation and release of histamine from mast cells. Histamine causes hypofenium, bronchoconstriction, vasodilatation.

    Fibrinogen– It is a soluble glycoprotein

    Fibrinogen undergoes proteolyticcleavage catalysed by thrombin to release small fibrinopeptides. This results in the formation of fibrin monomers which can stick together to form hard clots

    Its concentration in plasma is 0.2 – 04 g/dl. Fibrinogen is blood coagulation factor I. It should be noted that the number represent the order of discovery and not the order of action.

    The plasma is liquid medium of blood in which the cell components namely erythrocytes, leukocytes and platelets are suspended. If blood containing anticoagulants e.g heparin potassium oxalate is centrifuged, the plasma separated out as a separatant while the cells remain at the bottom. The names and functions of plasma proteins can be listed as under. The term serum is applied to the liquid medium which separates out after the blood coagulates. Serum does not contain fibrinogen and other clotting factors. This is the main difference between plasma and serum (The presence and absence of fibrinogen).


    Biochemistry for Dental Students

    • 1. Proteins are nitrogeneous macromolecules composed of many amino acids.

    • 2. Proteins are most abundant organic macromolecules widely distributed in plants and animals.

    • 3. They perform several dynamic functions in the oraganisms.

    • 4. Proteins are polymers of α amino acids.

    • 5. Proteins are classified in three bases—

      • a. On the basis of chemical nature.

      • b. On the nutritional basis.

      • c. On functional basis

  • 6. The structure of proteins is divided into four levels of organization. The primary structure represents linear sequence of acids. Twisting of peptide chain in secondary structure. Tertiary structure is equal to the three dimensional structure of a functional protein and the quarternary structure constitutes the assembly of similar dissimilar polypeptide subunits.

  • 7. The proteins possess physical as well as chemical properties.

  • 8. There are three group tests employed in lab to detect proteins. These are precipitation reactions, coagulation reaction and colour reactions.

  • 9. Heat coagulation test is most commonly employed to detect the presence of albumin in urine.

    • 10. The total concentration of plasma protein is about 7 – 7.5 gm.

    • 11. Electrophoresis seperates plasma proteins into five distinct bands namely albumin, α 1 ,α 2 , β and γ globulins.

    • 12. Albumin is the major constituent of plasma proteins with a concentration 3.5 – 5 gm /dl. Albumin performs cosmotic, transport and nutritive functions.

    • 13. α 1 -antitrypsin is a major constituent of α 1 globulin fraction. It’s deficiency has been emplicated in emphysema.

    • 14. Haptoglobin (Hp) binds with free hemoglobin (Hb) that spills into plasma due to hemolysis.

    • 15. Immunoglobulins are specialized proteins to defend the body against the foreign substances. They are associated with globulin fraction of plasma proteins.

    • 16. Five classes of immunoglobulins namely IgG , IgA, IgM, IgD and IgE are found in humans. IgG is most abundant and is mainly responsible for humoral immunity. IgA protects body surfaces. IgM serves as first line of defense for humoral immunity while IgEis involved in allergy, hypersensitivity and anaphylasis.

    • 17. Blood clotting is the body’s major defense mechanism against blood loss. Fibrinogen is blood coagulation factor number I. Finally, fibrinogen is converted fibrin clot.


    Amino Acids

    (The building blocks of proteins)

    The human body produces an impressive amount of macromolecules which are the polymers made up of monomer units. These large polymers may be carbohydrates, lipids, nucleic acids or proteins. In case of carbohydrates the monomer units are sugar derivatives. In case of lipids, these are fatty acids, in case of nucleic acids the monomers are nucleotides and in case of proteins these monomer units are amino acids. So, the amino acids as the name implies have got amino as well as carboxylic group. The amino acids can be defined as monomeric units or building blocks of proteins. Although about 300 amino acids are present in nature, but complete hydrolysis of protein produces about 20 L-α amino acids. The same 20 amino acids are present in all the forms of life.

    The L-α amino acids have a general formula.

    CHAPTER 4 Amino Acids (The building blocks of proteins) The human body produces an impressive amount

    R is called side chain. In case of glycine the side chain is H.

    The 20 L-α amino acids are glycine, alanine, serine, cystiene, threonine, valine, lucine, isoleucine, aspartic acid, glutamic acids, lysine, hydroxy lysine, phenylalanine, tyrosine, methionine, arginine, tryptophan, histidine, proline, hydroxyproline.


    The classification and structure of amino acids is inter related.

    • I. On the basis of nature of R.

    II. On the basis of their reaction in solution. III. On the basis of number of amino and acidic group.


    Biochemistry for Dental Students

    IV. On the basis of their chemical nature. V. On nutritional basis VI. On the basis of Fate.

    I. On the Basis of Nature of R

    On the basis of nature of R the amino acids are classified as:

    Classification on the basis of nature of side chain

    • 1. Side chain is H (R=H)–Glycine

    • 2. R=CH 2 –Alanine

    • 3. Alcoholic–Serine threonine

    • 4. Sulphur containing–Cysteine, cystine, methionine

    • 5. Acidic–Aspartic acid, glutamic acid

    • 6. Basic–Lysine, hydroxyl lysine

    • 7. Branched–Valine, leucine, isoleucine

    • 8. Heterocyclic–Tryptophan, histidine, arginine

    • 9. Aromatic–Tyrosine, phenylalanine, tryptophan

    10. No free NH 2 group proline, hydroxyproline

    11. Dimers–Cystine

    II. Reaction in Solution

    40 Biochemistry for Dental Students IV. On the basis of their chemical nature. V. On nutritional

    III. On the Basis of number of Amino and Acidic Group.

    • 1. Monoamino monocarboxylic acids–Neutral

    • 2. Diamino monocarboxylic acids–Basic

    • 3. Monoamino dicarboxylic acids–Acidic

    • 4. Diamino dicarboxylic–Neutral

    Amino Acids (The building blocks of proteins)


    IV. On the Basis of Chemical Nature the Amino Acids are Classified as Below

















    GALVI = Glycine,alanine,lysine,valine,isoleucine

    • V. On Nutritional Basis

    Essential and nonessential amino acids.

    • a. Essential amino acids are those which cannot be synthesized by our body and which should be taken in our diet. They include, methionine, arginine, threonine, tryptophan, valine, isoleucine, leucine, phenylalanine, lysine.

    • b. Non-essential amino acids: These are synthesized by our body and not to be taken in our diet essentially. The remaining all except this are belonging to this category.

    • c. Semi-essential: They are the growth promoting factors. During pregnancy lactation these become essential because they are synthesized in our body and the quality during. GPL = Growth pregnancy lactation is insufficient. They are the growth promoting factors. During pregnancy and lactation these become essential. G – Growth P – Pregnency L – Lactation.

    VI. On the Basis of Fate

    Amino Acids (The building blocks of proteins) 41 IV. On the Basis of Chemical Nature the


    Biochemistry for Dental Students

    Occurrence of Amino Acid

    Till the standard amino acids are present in almost all protiens, primary wheat is rich in acidic amino acids, e.g. glutamate, asparate while collagen is rich in basic amino acids, e.g. lysine, histidine.

    The amino acids which do not occur in proteins:

    Due to lack of codon for protein synthesis. There are some compounds which do not occur or which never occur in proteins but they have got the same basic skeleton of amino acids. These are :–

    • 1. α amino butyrate – a neurotransmitter.

    • 2. β alanine (β amino acid (found in CoA)

    • 3. Orithine, citrulline (metabolites of urea cycle).

    • 4. DOPA (Dihydroxy phenylalanine) precursor for a pigment called as melanin.

    • 5. Tri-Iodo teraiodothyronine (T 3 -T 4 ) thyroid hormones.

    • 6. Taurine (Bile salt).

    Function of Amino Acids

    Apart from monomeric constituents of protein and peptides amino acids serve variety of


    • a. Some amino acids are converted to carbohydrate and called as glucogenic amino acids. Some amino acids are converted to fats and are ketogenic amino acids as we have seen in classification.

    • b. Specific amino acids give rise to specialized i. Tyrosine forms hormones, like thyroid hormones (T3-T4). Epinephrine. Non-epinephrine and pigment called melanin and catecholamine (Nervous regulator). ii. Tryptophan synthesizes a vitamin called niacin. iii. Glycine, arginine and methionine synthesize creatine. iv. Glycine and cystine help in synthesis of bile salts. v. Glutamate, cystine and glycine synthesize glutathione (glu, cys, gly). vi. Histidine changes to histamine (vasodilation). vii. In addition to tripeptide formation glycine also used in synthesis of heme. viii.Pyrimidines and purines use several amino acids for their synthesis such as aspartate, glutamate for pyrimidines and glycine, serine, aspartic acid and glutamine for purine synthesis.

    • c. Some amino acids are used as detoxicants of specific subject such as glycine, cysteine.

    • d. Metheonine transfers methyl group to various group of transmethylation.

    • e. Cysteine and methionine are sources of sulphur.

    Amino Acids (The building blocks of proteins)


    Amino Acids (The building blocks of proteins) 43 Fig. 4.1: Existence of amino acids as cation,

    Fig. 4.1: Existence of amino acids as cation, anion and zwitteion


    Physical Properties (Fig. 4.1)

    • 1. They are colourless, crystalline substances more soluble in water then in other polar solvents such as ethanol and insoluble in non-polar solvent.

    • 2. They have high melting point usually more than 200°C.

    • 3. The aromatic amino acids absent UV light.

    • 4. Taste: Amino acids may be sweet, e.g. glycine; alanine valine, tasteless, e.g. leucine, bitter e.g. arginine. Sodium glutamate is salt of glutamic acid which is used in flavouring agent in food industry which increases taste and flavour.

    • 5. Optical properties: All the amino acids except glycine show optical isomerism because almost all have one asymmetric carbon.

    • 6. Ampholytes: As we know that amino acids have NH 2 as well COOH group so they can accept as well as donate one proton. Hence, they are regarded as ampholytes.

    • 7. Zwitterion: Amino acids have a property that in highly acidic pH they act as cation (+ve charged) while in highly alkaline medium they act as anion (-ve charged). So they are Zwitter molecules i.e. hybrid of + (positive) and – (negative) charges at a particular pH i.e. is isoelectric pH (As we can see in Fig 4.1).

    • 8. Chemical properties : The amino acids show following chemical properties

      • 1. Due to COOH group

      • 2. Due to NH 2 group


    Biochemistry for Dental Students

    • I. Reactions Due to COOH Group

    • a. Amino acids form esters alcohol with bases when COOH group is esterified

    44 Biochemistry for Dental Students I. Reactions Due to COOH Group a. Amino acids form esters
    • b. Decarboxylation: They undergo decarboxylation to form amines. This reaction is of significance because many biologically imp amines are formed by decarboxylation reactions.

    Examples are; Histidine to histamine: It is formed in injured tissues. It’s liberation is related to traumatic shock. Tyrosine to tyramine: It is involved in increasing blood presure.

    • c. Reaction with NH 3 — The amino acids react with NH 3 to form amide. e.g. aspartic acid + NH 3 – asparagine glutamic acid + NH 3 – glutamine.

    • d. Reduction to amino alcohol: This is achieved by the presence of lithium, aluminium hydride.

    44 Biochemistry for Dental Students I. Reactions Due to COOH Group a. Amino acids form esters

    II. Properteis Due to NH 2 Group

    • a. Salt formation with acids: The basic amino group reacts with mineral acids such as HCl to form salts like hydrochlorides. Glycine + HCl ===> Glycinehydrochloride

    • b. Formation of acyl derivatives: Amino group reacts with acyl anhydride or acyl halides such as benzoyl chloride and give acyl amino acids like benzoyl glycine (Hippuric acid) Incidentally this is one of the mechanism of detoxification in which glycine is used. This also forms the basis of liver function test.

    • c. Oxidation: Potassium permanganate or H 2 O 2 oxidizes the NH 2 group and converts the amino acid into imino acid which reacts with water to form NH 3 and α keto acid.

    • d. Reaction with Formaldehyde: Formaldehyde reacts with NH 2 group to form methylene compound.

    Amino Acids (The building blocks of proteins)


    III. Properties of Amino acids

    Due to both amino as well as carboxylic groups. Both cations and anions of amino acids react with certain heavy metals and other ions to form chelated complexes (Fig. 4.2).

    Amino Acids (The building blocks of proteins) 45 III. Properties of Amino acids Due to both

    Fig. 4.2: Calcium glycinate

    Clinical Applications

    Chelates are nonionic, therefore amino acids can be used to remove calcium from bones and teeth.

    It is possible that amino acids resulting from break down of enamel and dentine could in this way form soluble calcium complexes, thereby causing Loss of calcium and formation of dental caries.


    A peptide consists of two or more amino acid residues linked by a peptide bond which is a covalent bond(A peptide of more than 10 called as polypeptides.)

    Biologically Active Peptides

    Some small peptides which have significant biological activity are formed as a result of hydrolysis of large proteins while some are formed during synthesis. Some important biologically active peptides are—

    • 1. Angiotensin I: When the kidney enzyme renin acts on plasma globulin fraction to liberate a decapeptide known as angiotensin I which has got a slight effect on blood pressure.

    • 2. Angiotensin II: It consists of 8 amino acids and is formed by splitting of 2 amino acids from angiotensin I. It has a prominent effect on blood pressure. It also stimulates thirst, dilation of blood vessels of voluntary muscles and brain increased secretion of aldosterone takes place.

    • 3. Angiotensin III: It is of seven amino acids formed from angiotensin II by removal of aspartic acid has a role in pathology of hypertension.

    • 4. Antibiotics: Panicillin, actinomycines, chloramphenicol are all peptides. Tyrocidine and granulene contain D phenylalanine and ornithine which is absent in protein.


    Biochemistry for Dental Students

    • 6. Kellidin: One and two are decapeptides and show the relaxant effect on smooth muscles.

    • 7. Carnosine: Dipeptide (Histidine and alanine ) of voluntary muscles.

    • 8. Glutathione: It is a tripeptide consisting of glutamic acid, cystiene and glycine.

      • 1. It is easily converted to disulphide form and involved in oxidation-reduction reaction.

      • 2. By donating H 2 it helps to destroy H 2 O 2 and other peroxides in cells.

      • 3. Many –SH group containing enzymes are also protected by glutathione against oxidation.

  • 9. Hormones Gastrin secretion pancreozymin: Hormones of digestive tract. These stimulate secretion of bile and other digestive enzymes. Oxytocin vasopressin: Octapeptide containing 8 amino acids found in pitutary gland oxytocin acts on uterine muscles and involved in parturation and ejection of milk while vasopressin influences reabsorption of water by distal and collecting tubules.

    • 1. Amino acids are monomeric constituents of proteins.

    • 2. There are 20 amino acids which are obtained on complete hydrolysis of proteins found in nature.

    • 3. Amino acids possess two functional groups namely (-COOH) and amino (-NH 2 ). In the physiological system, they exist as dipolar ions commonly refered to as zwitterions.

    • 4. The amino acids are classified into different groups based on their structure, chemical nature, nutritional requirement and metabolic fate.

    • 5. Besides the 20 standard amino acids present in proteins, there are several non-standard amino acids. These include ornithine citrulline and dopa.

    • 6. All amino acids show properties due to amino groups, carboxlic groups and due to both of them.

    • 7. In addition to protein and amino acids, several peptides perform, biologically important function. These include glutathione, oxytocin, vasopressin.



    (The living catalysts)


    Enzymes are organic catalytic agents, protein in nature, produced by living cells but for their whole action presence of living cells is not necessary.

    Special Features of Enzymatic Activity

    • 1. If oxidation-reduction or hydrolytic action is done in laboratory, it will require a great deal of heating and addition of corrosive quantity of acids or alkalies, and yet long time, But within our body the enzymes accomplish hydrolysis, oxidation, reduction, etc. a. At body temperature b. Without injuring cells c. Speedily. Chemical reactions usually produce side products but enzymatic catalysis does not produce any side products. Thus, we can say that enzyme catalysis is much more efficient than man made catalysis.

    • 2. Enzymes are highly specific, thus sucrase splits sucrose not maltose although both of them are closely similar in structure, similarly maltase splits maltose but not the sucrose. However, some enzymes are there which can act on chemically close substrates (where substrate a compound on which the enzyme acts).

    • 3. The enzymes also show optical specificity thus the enzymes in our body which can act on L-amino acids cannot act on D amino acids.

    Factors Influencing Enzyme Activity

    • I. Temperature.

    II. pH.

    III. Effect of ion. IV. Concentration of substrate.

    • V. Concentration of enzyme


    Biochemistry for Dental Students

    I. Temperature: Most of enzymes in our body act best around our body temperature around 38°C. If the temperature decreases, the efficiency of enzymes also falls at around 0°C, the enzymes become remarkably inactive around – 20°C, but at normal temperature again the efficiency is regained. The optimal temperature is that temperature at which the enzyme acts best (Fig. 5.1).

    II. Effect of PH: Every enzyme has an optimal pH, that is a PH in which, the enzyme acts best. The PH for pepsin, trypsin and salivary amylase are 1.5, 8.0, 6.8 respectively. Outside its optimal PH the enzyme loses its activity or efficiency. It is well known that acidosis is dangerous and if not concerned with treatment lead to death. The reason is that as acidosis advances, most of the enzymes in our body become insufficient and eventually all chemical reactions stop which lead to death.

    48 Biochemistry for Dental Students I. Temperature: Most of enzymes in our body act best around

    Fig. 5.1: Showing effect of temperature on enzyme activity

    III. Effect of Ions: Some enzyme reactions cannot proceed unless ions like mg ++ , zn ++ , mn ++ are present in reactions medium, e.g. Cl ions enhance the action of salivary amylase.

    48 Biochemistry for Dental Students I. Temperature: Most of enzymes in our body act best around

    Fig. 5.2: Showing effect of substrate concentration on enzyme activity

    Enzyme (The living catalysts)


    IV. Concentration of substrate: The concentration of substrate is directly proportional to the velocity of reaction. Further increase of substrate does not cause increase of the rate of reaction (Fig. 5.2).

    V. Concentration of enymes: Within fairly wide limits the speed of an enzymatic reaction is proportional to the enzyme concentration. This can be shown to hold for many enzymes systems, provided interfering conditions do not develop and the substrate concentration is maintained constant (Fig. 5.3).

    Enzyme (The living catalysts) 49 IV. Concentration of substrate: The concentration of substrate is directly proportional

    Fig. 5.3: Showing effect of enzyme concentration on enzyme activity

    Mechanism of enzyme action: The enzyme combines with its substrate to form enzyme

    substrate complex within the complex the substrate breakdown into products and then the enzyme dissociates from the substrate. Using symbol it can be expressed as:

    E + S


    < ________

    E S


    < ________

    Where letter E, S and P stand for enzyme, substrate and products respectively. The symbolstands for reversibility. This theory originally was introduced by machalies manton which is not universally agreed.

    VI. Koshald hypothesis

    (Induced fit model). D.E. Koshald has introduced a hypothesis called, the induced fit hypothesis. An enzyme when, not occupied by the substrate has a particular geometrical shape when the enzyme is attached with substrate, the shape of enzyme molecule alters slightly and because of this alteration of substrate (a molecule which also has a fixed geometrical shape) can fit in properly into the enzyme molecule. This is called an induced fit. In this altered configuration however the enzyme is unstable (As shown in Fig 5.4).


    Biochemistry for Dental Students

    50 Biochemistry for Dental Students Fig. 5.4: showing induced fit hypothesis Enzyme Enhibition Suppression of enzyme

    Fig. 5.4: showing induced fit hypothesis

    Enzyme Enhibition

    Suppression of enzyme action is called as enzyme inhibition. The inhibition is classified as follows—

    50 Biochemistry for Dental Students Fig. 5.4: showing induced fit hypothesis Enzyme Enhibition Suppression of enzyme

    a. Competitive inhibition: The inhibitor molecule which usually has a very closely resembling chemical configuration with the substrate molecule and yet is chemically a separate molecule

    has affinity for the active sight of the enzyme, therefore both the normal substrate molecule as well as the inhibitor molecule compete for the same active site and the active site may be occupied by the inhibitor molecules. As a result the normal substrate molecule cannot get attached with enzyme molecule forming a complex instead of ES , EI , speaking symbolically. E + I ———EI b. Uncompetitive inhibition: In this type of inhibition , the binding between the enzyme and normal subsrate occurs as usual , but now an inhibitor molecule becomes attached to the enzyme substrate complex and this stops the breaking down of the substrate. Enzyme complex symbolically it can be written as–

    E + S ES + I


    > ES > ES I


    Enzyme (The living catalysts)


    (c) Noncompetitive Inhibition: A non-competitive inhibitior binds with the enzyme at a site other than the active site and as a result causes deformation of the enzyme molecule and there occurs inhibition of enzyme. E+I —— E I Irreversible: Treatment with iodo acetic acid causes alkylation of some enzyme and enzymatic activity. So in this type of inhibition the enzymatic power is permanently destroyed.

    Nomenclature of Enzyme

    In the past, some names entered into use, thus pepsin, trypsin and chymotrypsin are well

    established names. In some cases the suffix-ase is added to the name of substrate on which, the enzyme acts. Thus, there are such names like—


    Acts on sucrose


    Acts on maltose


    Acts on urea


    Acts on arginine


    Acts on lecithin


    The enzymes are classified into six major classes. Each class on its own represents the general type of reaction bought about by the enzyme of that class (Fig. 5.5 and Table 5.1).

    Enzyme (The living catalysts) 51 (c) Noncompetitive Inhibition: A non-competitive inhibitior binds with the enzyme at

    Fig. 5.5: Showing classification of enzymes

    • 1. Oxidoreductase: These enzymes catalyse the oxidation and reduction of their substrates e.g. succinic, dehydrogenase, oxidizing succinic acid into fumaric acid.

    • 2. Transferase: These enzymes catalyse the transfer of some groups or radical from one molecute to another molecule, e.g. glutamate pyruvate transaminases transfers NH 2 (amino) group from glutamic acid to pyruvic acid. As a result glutamic and pyruvic acids are converted into α ketoglutaric acid and alanine respectively.

    • 3. Hydrolases: These enzyme cause splitting of molecule by hydrolysis, e.g. pepsin, trypsin, lipase

    • 4. Lyase: They remove groups from the substrates by methods other than hydrolases, e.g. aldehyde lyases (aldolases).

    • 5. Isomerases: They cause conversion of substrate into its isomer. Phosphoisomerase

    Glyceraldehyde 3p < Phospho isomerase


    > Dihydroxy acetone phosphate.


    Biochemistry for Dental Students

    • 6. Ligase: Two substrates are linked together by the action of ligase

    52 Biochemistry for Dental Students 6. Ligase: Two substrates are linked together by the action of

    [OTHILL(First letter of each class) is the word which can be memorized to remember six classes of enzymes in the correct order.]

    Table 5.1: Showing enzyme class with example

    • 1. Oxidoreductases Alcohol dehydrogenase (alcohol:NAD+ Oxidoreducatase E.C.

    • 2. Transferases

    Oxidation ———> Reduction AH 2 + B ———> A + BH 2 Group transfer

    Hexokinase (ATP: D-hexose 6- A – X + B ———> A + B – X

    phosphotransferase, E.C., Transaminases, transmethylases, phosphorylase

    • 3. Hydrolases Lipase (triacylglycerol acyl hydrolase E.C., Choline esterase, acid and alkaline phosphatases, pepsin, urease

    Hydrolysis A – B + H 2 O ———> AH + BOH

    • 4. Lyases

    Addition ———> Elimination

    Aldolase (ketose 1-phosphate aldehyde-

    A – B + X – Y ———> AX - BY

    lyase, E.C., fumarase, histidase

    • 5. Isomerases

    Interconversion of isomers

    Triose phosphate isomerase A ———> A’

    (D-glyceraldehyde 3-phosphate etoisomerase,

    E.C., retinine isomerase, glucose phosphate isomerase

    • 6. Ligases Glutamine synthetase (L-glutamate ammonia ligase, E.C., acetyl CoA carboxylase, succinate thiokinase

    Condensation (usually dependent on ATP) A + B———> A – B

    • For one enzyme in each class, systematic name along with E.C. number is given in the brackets

    Division of Enzymes

    Chemically the enzymes can be divided into two groups.

    Enzyme (The living catalysts)


    • A. Simple protein enzyme consisting of simple protein

    • B. Complex protein enyme or conjugated enzyme consisting of a protein part apoenzyme and a prosthetic group coenzyme. Combination of apoenzyme with conenzyme constitutes the holoenzymes, thus holoenzyme is a conjugated enzyme.



    Coenzymes are heat stable dialyzable, nonprotein organic molecules and the prosthetic groups of enzyme (Fig. 5.6).

    Enzyme (The living catalysts) 53 A. Simple protein enzyme consisting of simple protein B. Complex protein

    Fig. 5.6: Classification of coenzymes

    Functions of Coenzymes (Table 5.2)

    • 1. The function of coenzymes is usually to accept atoms or groups from a substrate and transfer them to other molecules.

    • 2. They are less specific than enzymes. Some coenzyme can act as such in No. of different reactions.


    Biochemistry for Dental Students

    Table 5.2: Increases in plasma (serum enzymes in the diagnosis of diseases


    Normal value

    Diseases in which increased

    • I. Digestive enzymes

    80-180 Somogyi units/dl or


    • 2.5 – 5.5 μKat


    • 0.2 – 1.5 IU/ I

    II. Transaminases

    Alanine transaminase ALT) or serum glutamate pyruvate transminase (SGPT) Aspartate transaminase (AST )or serum glutamate oxaloacetate transaminase (SGOT)

    III. Phosphatases

    Alkaline phosphatase (ALP)(pH) optimum 9-10)

    3-40 IU/I or 40-250 nKat

    4-45 IU/I or 50-320 nKat

    In adults 3-13 King Armstrong (KA) units/dl or 25-90 IU/I or 500-1400 nKat

    Acid phosphatase (ACP) (pH optimum 4 – 6)

    In children 15-30 KA/dl (due to higher 0.5-4 KA units/ dl or 2.5 -12 IU/I or 10-100 nKat. Tartarate labile ACP 0-0.9 KA units/dl

    IV.Enzymes of carbohydrate metabolism

    Aldolase isocitrate dehydrogenase (ICD) Lactate dehydrogenase (LDH)

    • V. Miscellaneous enzymes

    2-6 IU/I 1-4 IU/I 50-200 IU/I or 1-5 μKat

    Acute pancreatitis, mumps (acute

    parotitis), obstruction in pancreatic duct,

    severe diabetic ketoacidosis. Acute pancreatitis, moderate elevation in carcinoma of pancreas. Acute hepatitis (viral or toxic), jaundice, cirrhosis of liver.

    Myocardial intarction, liver diseases, liver cancer, cirrhosis of liver.

    Bone diseases (related to higher osteoblastic activity)-rickets, Pagets disease, hyperparathyroidism, carcinoma of bone.

    Liver diseases obstructive jaundice (cholestasis), infective hepatitis, cirrhosis of liver. Prostatic carcinoma, i.e. cancer of prostate gland (tartarate liabile ACP serves as a marker for diagnosis and follow up) Paget’s disease, Gaucher’s disease.

    Muscular dystrophy, liver diseases, myocardial infarction, myasthenia gravis, leukemias .Liver disease (inflammatory toxic or malignant)Myocardial infarction actue infective hepatits, muscular dystrophy, leukemia, pernicious anaemia.

    Creatine kinase (CK)

    10-50 IU/I

    Myocardial infarction (CK useful for early detection), muscular dystrophy, hypothyroidism, alcoholism.

    Creatine Phosphokinase

    2-10 IU/I

    Nephroidism, alcoholism.

    (CPK) Choline esterase (ChEI)

    2-15 IU/I

    Nephrotic syndrome, myocardial infarction

    5 Nucleotidase or nucleo- tide phosphatase (NTP)

    5-40 IU/I

    Hepatitis, obstructive jaundice, tumors.

    Glutamyl transpeptidase (GGT)

    20-50 mg/dl

    Alcoholism, infective hepatitis , obstructive jaundice.


    Bacterial infections, collagen diseases,


    cirrhosis, pregnancy

    Enzyme (The living catalysts)


    • 4. NAD and NADP coenzymes function as hydrogen acceptors in dehydrogenation reactions.

    • 5. The chief function of COA is to carry acyl groups and they are used in acetylation decarboxylation of pyruvic acid and synthesis of fatty acid and in acelytation reactions.

    • 6. The function of TPP (cocarboxylase) is to cartry active aldehyde (R CH OH)- group is involved in transamination reaction.

    • 7. The chief function of tetrahydrofolic acid is as a carrier of formate and it is used in the synthesis of peruvines and pyramidenes.

    • 8. The chief function of pyridoxal phosphate is involved in the transmination reaction.

    • 1. Enzymes are biocatalysts, proteinous in nature.

    • 2. Enzyme catalysis is much more efficient than man made catalysts.

    • 3. They are classified into six major classes—oxidoreductases, transferases, hydrolases, lyases isomerases, and ligases.

    • 4. Factors like concentration of enzymes, substrate concentration, temperature, pH, influence enzyme activity.

    • 5. Enzyme activities are inhibited by reversible (competitive, uncompetitive and non- competitive) and irreversible manner.

    • 6. Many enzymes require, the presence of non-protein substances called (cofactor) coenzymes for their action, most coenzymes are derivative of B-complex vitamins (NAD+ , FAD, TPP).

    • 7. The mechanism of enzyme action is explained by lock and key model and more recently induced fit model (of Koshald).


    Digestion, Absorption and Metabolism of Carbohydrates

    (Burning of instant fuel)


    Dietary carbohydrates principally consist of the polysaccharides, (starch and glycogen). It also contains disaccharides (sucrose lactose, and maltose) and in small amount monosaccharides like fructose; and glucose–Liquid food materials like milk, soup, fruit juice escape digestion in mouth as they are swallowed, but solid food stuffs are masticated thoroughly before, and then they are swallowed.

    Digestion in Mouth

    Digestion of carbohydrate starts in the mouth, where they come in contact with saliva; during mastication saliva contains a carbohydrate splitting enzyme called salivary amylase (ptyalin).

    Action of Ptyalin (Salivary Amylase)

    It is α amylase which requires Cl ions for activation and optimum pH 6.7 (range 6.6 to 6.8). The enzyme hydrolyses α- 1 —> 4 glycosidic linkage at random, deep inside polysaccharide molecules like starch, glycogen and dextrins, producing smaller molecules maltose, glucose and trisaccharide maltotriose. Ptyalin action stops is stomach when pH falls to 3.0. Amylase Starch glycogen and dextrins —————> Glucose, maltose maltotriose (As shown in Fig 6.1)

    Digestion in Stomach

    Practically no action. No carbohydrate splitting enzymes available in gastric juice. Some dietary sucrose may be hydrolyzed to equimolar amounts of glucose and fructose by HCl.

    Digestion, Absorption and Metabolism of Carbohydrates (Burning of instant fuel)


    Digestion in Duodenum

    Food bolus reaches duodenum from stomach, where it meets the pancreatic juice. Pancreatic juice contains carbohydrate splitting enzyme pancreatic amylase (also called amlyopsin) similar to salivary amylase.

    Action of Pancreatic Amylase (Fig. 6.1)

    It is also an amylase optimum pH 7.1, like ptyalin, it also requires Cl for activity. The enzyme hydrolyses α - 1- 4 glycosidic linkage situated well inside polysaccharide molecule. Other criteria and end products of action similar to ptyalin.

    Digestion in small intestine: Action of intestinal juice

    Intestinal amylase: This hydrolyses terminal α - 1- 4 glycosidic linkage in polysaccharide and oligosaccharide molecules liberating free glucose molecule. • Lactase:– It is αβ galactosidase, its pH range is 5.4 to 6.0. Lactose is hydrolysed to equimolar amounts of glucose and galactose.

    Lactase Lactose ——————> Glucose + Galactose

    Isomaltase: It catalyses hydrolysis of α - 1- 6 glycosidic linkage, thus splitting limit dextrin at the branching points and producing maltose and glucose.

    Digestion, Absorption and Metabolism of Carbohydrates (Burning of instant fuel) 57 Digestion in Duodenum Food bolus

    Fig. 6.1: Showing digestion of carbohydrates


    Biochemistry for Dental Students

    Maltose:– The enzyme hydrolyses the α - 1 – 4 glycosidic linkage between glucose units in maltose molecule liberating equimolar quantities of two glucose molecules. Its pH range is 5.8 to 6.2.

    Maltose Maltose ———————— Glucose + Glucose Sucrase:– pH range 5.0 to 7.0. It hydrolyses sucrose molecule to form equimolar quantities of glucose and fructose.

    Sucrase Sucrose ———————— Glucose + Fructose


    It is observed from above that carbohydrate digestion is complete when the food material reach small intestine and all complex dietary corbohydrates like starch and glycogen and the disaccharides are ultimately converted to simpler monosaccharide. All monosaccharide products of digestion of dietary carbohydrates are practically completely absorbed almost entirely from the small intestine. It is observed that some disaccharides which escape digestion may enter the cells lining the intestinal lumen and hydrolyzed within cells. No carbohydrates higher then the monosaccharide can be absorbed directly into the bloodstream in normal health and if administered parenterally, they are eliminated as foreign bodies. Glucose and galactose are absorbed very fast, fructose and mannose at intermediate rate and pentoses are absorbed slowly. A galactose is absorbed more rapidly than glucose.

    Mechanism of Absorption

    There are two mechanisms suggested:

    • I. Active transport mechanism.

    II. Simple diffusion

    • I. Active Transport Mechanism

    Glucose and galactose are absorbed very rapidly and hence, it has been suggested that they are absorbed actively and it requires energy. • Fructose absorption is also rapid but not so much as compared to glucose and galactose but it is definitely faster than pentoses. Hence, fructose is not absorbed by simple diffusion alone and it is suggested that some mechanism facilitates its transport called facilitate diffusion. It requires a carrier protein but no requirement of energy.

    II. Simple Diffusion

    This is dependent on sugar concentration gradients between the intestinal lumen, mucosal cells and blood plasma. All the monosaccharide are probably absorbed to some extent by simple passive diffusion sugars like pentose.

    Digestion, Absorption and Metabolism of Carbohydrates (Burning of instant fuel)


    Sugars like pentoses are passively absorbed by simple diffusion, no requirement of carrier protein as well as energy.

    Metabolism of Carbohydrates

    Carbohydrates are the major source of energy for living cells. The monosaccharide glucose is the central molecule in carbohydrate metabolism since all the major pathways of carbohydrate metabolism are connected with it major pathways of carbohydrate metabolism:

    • 1. Glycolysis: Oxidation of glucose to pyruvate and lactate.

    • 2. Citric acid cycle: The oxidation of acetyl CoA to CO 2 .

    • 3. Gluconeogenesis: The synthesis of glucose from non carbohydrate sources.

    • 4. Glycogenesis: The formation of glycogen from glucose.

    • 5. Glycogenolysis: The breakdown of glycogen to glucose and then to lactate and pyruvate.


    It is derived from a greek word glycose–sweet, Lysis – breakdown. It is defined as the sequence of reactions converting glucose to pyruvate or lactate with production of ATP. Glycolysis is a universal pathway in the living cells. It takes place in all cells of the body. It takes place in presence of oxygen (aerobic) and in absence of oxygen (anaerobic) All enzymes are found in the cytosomal fraction of all cells. The end products are pyruvate and lactate in aerobic and anaerobic condition respectively.

    Reaction of Glycolysis

    The pathway of glycolysis can be divided into three distinct phases—

    • I. Energy investment phase or priming phases. II. Splitting phase

    III. Energy generation phase.

    • I. Energy Investment Phase

    Glucose is phosphorylated to glucose 6P in presence of enzyme hexokinase or glucokinase. This is an irreversible reaction depending upon ATP and Magnesium ion. Glucose 6P undergoes isomerization to fructose 6P in presence of an enzyme phosphohexose isomerase. • Fructose-6-phosphate is again phosphorylated to fructose 1, 6, biphosphate the enzyme required for it is phosphofructokinase again ATP is converted to ADP.

    II. Splitting Phase

    The six carbon compound fructose 1, 6 biphosphate in spits to two 3 carbon compound glyceraldehyde 3P and dihydroxy acetone phosphate by the enzyme aldolase.


    Biochemistry for Dental Students

    In presence of enzyme isomerase, there occurs isomerization of dihydroxy acetone phosphate into glyceraldehyde 3P. Thus now there are two molecules of glyceraldehyde 3 P.

    III.Energy Generation Phase

    Glyceral dehyde 3P dehydrogenase converts glyceraldehydes 3P to 1, 3 bisphosphoglycerate here NAD+ is converted to NADH+H. Thus now 6ATP are synthesized.

    60 Biochemistry for Dental Students • In presence of enzyme isomerase, there occurs isomerization of dihydroxy

    Fig. 6.2: Showing reaction of glycolysis

    Digestion, Absorption and Metabolism of Carbohydrates (Burning of instant fuel)


    • Phosphoglycerate kinase acts on 1, 3 bisphosphoglycerate resulting in synthesis of ATP and formation of 3 phosphoglycerate. • Three phosphoglycerate is converted to 2 phosphoglycerate by phosphoglycerate mutase Mg ++ is required. • By enolase phosphoenol pyruvate is generated from 2 phosphoglycerate Mg ++ are required for this reaction. • Phosphoenol pyruvate is converted to pyruvate by pyruvate kinase. Mg ++ ions are required ADP is converted to ATP. Three steps where the enzyme kinase is utilized (i) hexokinase (ii) phosphofructokinase (iii) pyruvate kinase are irreversible, rest all reactions are reversible (Fig. 6.2 and Table 6.1).

    Table 6.1: Energetics of glycolysis in aerobic condition




    Enzymes required for reactions


    2 ATP

    1st Step



    3rd Step



    6 ATP

    6th step

    Glyceraldehyde 3P dehydrogenase



    7th Step

    Phosphoglycerate kinase



    10th step

    Pyruvate kinase

    Energy consumption is

    10 ATP


    subtracted from total

    -2 ATP

    energy production Net gain

    8 ATP

    Conversion of Pyruvate to Lactate

    Depending upon the presence or absence of oxygen, i.e. aerobic and anaerobic conditions respectively, the fate of pyruvate produced in glycolysis is either towards Krebs’ cycle (aerobic) or it is reduced to lactate by NADH in presence of an enzyme lactate dehydrogenase. The NADH utilized in this step is obtained from the reaction catalysed by glyceraldehyde 3-phosphate dehydrogenase. The formation of lactate allows the regeneration of NAD which can be reused by glyceraldehyde 3P dehydrogenase so that the glycolysis can take place even in absence of oxygen to supply ATP.


    The details of ATP generated in aerobic condition is given in the above chart, that is 8 ATP, are synthesized in aerobic condition while in anaerobic condition 2 ATP are synthesized because NADH is utilized by lactate dehydrogenase to carryout conversion of pyruvate to lactate.


    Biochemistry for Dental Students

    Oxidation of pyruvate to Acetyl CoA

    Pyruvate is oxidatively decarboxylated to acetyl CoA before entering the Krebs’ cycle. The reaction is catalysed by a multienzyme complex PDH that is pyruvate dehydrogenase complex which is found only in mitochodria. The multienzyme complex PDH requires five coenzymes namely TPP, lipomide, FAD, coenzyme A, and NAD (Fig. 6.3).

    62 Biochemistry for Dental Students Oxidation of pyruvate to Acetyl CoA Pyruvate is oxidatively decarboxylated to

    Fig. 6.3: Connecting link between glycolysis and Krebs’ cycle


    There are four names of same cycle and these are citric acid cycle, Krebs’ cycle, and tricar- boxylic acid cycle, or TCA – Cycle. This cycle is the most important metabolic pathway as far as the supply of energy is