AS Biology Unit F212 Enzymes

Enzymes
Specification
State that enzymes are globular proteins with a specific tertiary structure which catalyse metabolic reactions in living organisms State that enzyme action may be intracellular or extracellular Describe with the aid of diagrams the mechanism of action of enzyme molecules with reference to specificity, active site, lock and key hypothesis, induced-fit hypothesis, enzyme-substrate complex, enzyme-product complex, product complex and lowering of activation energy Describe and explain the effects of pH, temperature, enzyme concentration and substrate concentration on enzyme activity Describe how the effects of pH, temperature, enzyme concentration and substrate concentration on enzyme activity can be investigated experimentally Explain the effects of competitive and non-competitive inhibitors on the rate of enzyme-controlled reactions, with reference to both reversible and nonreversible inhibitors Explain the importance of cofactor of coenzymes in enzyme controlled reactions State that metabolic poisons may be enzyme inhibitors and describe the action of one named poison State that some medicinal drugs work by inhibiting the activity of enzymes

Introduction
D D Enzymes ! "uick overview introducing terms #$iology % ! &'()min*

Definition A catalyst is a substance which alters the rate of a chemical reaction without itself undergoing a permanent change As they are not altered by the reactions they catalyse they can be used again and again and are effecti!e in !ery small "uantities # B $atalysts cannot cause reactions to occur% but only speed up ones that would occur anyway

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AS Biology Unit F212 Enzymes

Enzyme structure and function

$omple. +/d globular proteins% some of which ha!e associated molecules e g haem in catalase Enzymes are specific i e they will normally only catalyse one reaction Enzyme molecule is usually much bigger than the substrate molecules it wor0s on% so only a small part of the molecule comes into contact with the substrate this region is called the acti!e site 1ften this only consists of a few amino acids 2+ 123 ,he shape of the acti!e site is maintained by the rest of the molecule ,he shape of the acti!e site is complementary to the substrate loc0 and 0ey mechanism Draw #ow clear that the shape of the acti!e site in some enzymes changes when the substrate binds induced fit Draw Enzyme substrate comple. Anabolism building larger molecules our of smaller ones e g proteins from amino acids $atabolism brea0ing 2cutting3 large molecules into smaller ones e g digestion of starch into glucose 2http+,,highered'mcgraw-hill'com -hapter & animation of lysosomes* Enzymes can wor0 inside cells 2intracellular3 to regulate metabolic reactions% or can be secreted from the cell to wor0 outside 2e.tracellular3 e g digesti!e enzymes 4igesti!e enzymes are either secreted in an inacti!e form or are contained in !esicles to pre!ent them destroying the contents of the cell

Enzymes and metabolic pathways

-etabolism the sum total of all the chemical reactions occurring in cells 5ith many hundreds of reactions ta0ing place in a single cell it is essential for a !ery structured system of control $ells contain organelles and enzymes are often bound to these internal membranes in a !ery precise order ,his increases the chances of the enzyme coming into contact with their appropriate substrates ,he organelles also may ha!e the specific conditions e g p6 for the enzymes to wor0 best -etabolic reactions usually happen in a series of small steps% each catalysed by a different enzyme 7nborn error of metabolism are diseases caused by the lac0 of a functioning specific enzyme in a metabolic se"uence e g phenyl0etonuria is a disease where the enzyme that brea0s down the amino acid phenylalanine is missing and any build up will cause irre!ersible damage to the ner!ous system and to brain de!elopment All newborns are screened for this disease ,reatment is by limiting the amount of phenylalanine in the diet

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AS Biology Unit F212 Enzymes

Classification of enzymes
Enzymes are catalysed into 8 groups according to the type of reaction they catalyse ,his is an internationally accepted classification

Enzyme group
1.idoreductases

Type of reaction catalysed

,ransfer of 1 and 6 atoms between substances i e all o.idation reduction reactions ,ransfer of a chemical group from one substance to another 6ydrolysis reactions

Enzyme examples
4ehydrogenases 1.idases

,ransferases 6ydrolases

,ransaminases &hosphorylases &eptidases 9ipases &hosphatases 4ecarbo.ylases 7somerases -utases Synthetases

9yases 7somerases 9igases

Addition or remo!al of a chemical group other than by hydrolysis ,he rearrangement of groups within a molecule Formation of bonds between two molecules using energy deri!ed from the brea0down of A,&

Each enzyme is gi!en 2 names: A systematic name% based on the 8 classifications ,hese names are usually long and complicated A tri!ial name which is shorter and easier to use Start with the name of the substrate on which the enzyme acts e g succinate Add the name of the type of reaction which it catalyses e g dehydrogenation $on!ert the end of the last word to an ase suffi. e g dehydrogenase ,his would gi!e succinate dehydrogenase

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AS Biology Unit F212 Enzymes

Enzymes and activation energy

7n chemical reactions energy is re"uired to brea0 the bonds in the reactants in order that they may then reform as the products ,he amount of energy re"uired to brea0 these bonds is termed the acti!ation energy and is pro!ided in the form of heat Enzymes wor0 by reducing the amount of heat needed to brea0 these bonds so the reaction ta0es place more easily .raph of activation energy and diagram of bonds breaking and re-forming'

Factors affecting enzyme activity

Temperature
Each enzyme has an optimum temperature at which it will wor0 -onsider some examples' Below this temperature the 0inetic energy of the enzyme and substrate molecules reduces and hence so will the rate of the reaction as the molecules do not come into contact as fre"uently Abo!e this temperature the protein will start to denature irre!ersibly and the shape of the acti!e site will change and not wor0 Draw graph of rate of reaction vs temperature and notice it is not a symmetrical shape

pH
Each enzyme has an optimum p6 at which it will wor0 -onsider some examples e'g' digestive enzymes' $hanges in p6 affect the ionisation of side groups in the aa;s% which will ha!e a 0noc0 on effect on the shape of the molecule 6ydrogen bonds will brea0 As the p6 mo!es away from optimum the molecule will denature -onsider some examples of enzymes working in different pH conditions e'g pepsin pH (, arginase pH /0 Some intracellular conditions can be different to the optimum p6 and so the enzyme acti!ity can be controlled Draw graph of rate of reaction vs pH and notice it is a symmetrical shape

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AS Biology Unit F212 Enzymes

Concentration
Enzyme concentration Acti!e site may be used again and again ,urno!er number < number of substrate molecules which an enzyme can act upon in a gi!en time !aries form many millions per minute e g catalase to a few hundred for a slow acting one =ate of reaction is directly proportional to the enzyme concentration pro!ided that there is an e.cess of substrate and temp and other conditions are good create the shape of graph that this describes ubstrate concentration At low concentrations not all acti!e sites are being used As substrate concentration rises more acti!e sites come into use 5hen all acti!e sites are being used enzyme concentration becomes a limiting factor create the shape of graph that this describes

Inhibitors
=e!ersible inhibitors act in 2 different ways 1nterpret the ( pictures following and describe how each might work+ Competitive inhibition

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AS Biology Unit F212 Enzymes

!on"competitive inhibition

#on/re!ersible inhibitors lea!e the molecule permanently damaged and so unable to carry out catalytic function e g mercury and sil!er ions cause disulphide bond to brea0 and hence shape of molecule changes

Coenzymes and #rosthetic groups

Some enzymes can only wor0 is another non/protein substance is present these are 0nown as co/factors Some cofactors are a part of the enzyme prosthetic group? others affect the enzyme on a temporary basis coenzymes and inorganic ion cofactors

#oisons and drugs

-any poisonous substances wor0 by inhibiting or o!er acti!ating enzymes e g potassium cyanide inhibits respiration by being a non/competiti!e inhibitor of the enzyme cytochrome o.idase Antibiotics wor0 by 0illing or inhibiting the growth of bacteria e g penicillin wor0s by inhibiting a bacterial enzyme that forms the cross lin0s in the cell wall of some bacteria hence pre!enting it from reproducing Sna0e !enom generally contains a coc0tail of to.ins and harmful enzymes e g phosphodiesterases interfere with the wor0ing of the heart% an inhibitor of the enzyme acetyl cholinesterase causes paralysis by interfering with ner!e transmission% hyaluronidase is a digesti!e enzyme that brea0s down connecti!e tissue # B ,he same enzyme inhibitor may act as both a poison and a drug depending on the amount of inhibitor and its location e g alcohol ta0en o!er a period of time is !ery damaging to the li!er but alcohol is also a treatment for ethylene glycol poisoning

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AS Biology Unit F212 Enzymes

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