ENZYME

dr. JANGKI HASHUMAL

DEPARTEMENT OF BIOCHEMISTRY FACULTY OF MEDICINE HASANUDDIN UNIVERSITY

DEFINISI NOMENKLATUR DAN KLASIFIKASI INTERAKSI ENZIM-SUBSTRAT KOFAKTOR DAN KOENZIM PENGARUH pH DAN SUHU CONTOH ENZIM SPESIFIK

DEFINISI
Enzim adalah biokatalisator Biological sistem hidup Substansi yang meningkatkan kecepatan reaksi kimia tanpa mengubah hasil

Biokatalisator
Protein dengan molekul besar Permit reactions to go at conditions that the body can tolerate Can process millions of molecules every second Are very specific react with one or only a few types of molecules (substrate) Substrate is a substance that is acted on by an enzyme

NOMENCLATURE AND CLASSIFICATION

Enzyme nomenclature is based on : What it reacts with How it reacts Add ase ending Examples : Lactase : enzyme that reacts with lactose Pyruvate decarboxylase : removes carboxyl from pyruvate

Enzyme usually written in trivial name but every enzyme has an official name from International Union of Biochemistry (Enzyme Nomenclature 1992) Based on the official nomenclature system, each enzyme has a full name and an enzyme commission number (E.C) derived in the position in the classification scheme Example : Hexokinase has the full name ATP: D-hexose 6phosphotransferase and the classification number E.C 2.7.1.1

Classification of enzymes
Based on type of reaction, enzymes have been classified to six major classes as follows : 1.Oxidoreductases : catalyze oxidationreduction reactions 2.Transferases : catalyze trnasfer of functional groups fron one molecule to another 3.Hydrolases : catalyze hydrolytic cleavage

4. Lyases : catalyze removal of a group from or addition of a group to a double bond, or other cleavages involving electron rearrangment 5. Isomerases : catalyzed intramoleculer rearrangement 6. Ligases : catalyzed reactions in which two molecules are joined

ENZYME-SUBSTRATE INTERACTION
UNCATALYZED REACTION

E N E R G Y

G SUBSTRATE

PRODUCT

Effect of enzyme on activation energy : All reaction must get over the activation energy hurdle

VELOCITY

CATALYZED REACTION

E N E R G Y

Substrate Product

Enzyme change how a reaction will proceed Enzyme reduces the activation energy And it makes the reaction faster

VELOCITY

Effect of substrate concentration:

For non-catalyzed reaction: Reaction rate increase with concentration For enzyme catalyzed reaction : Also increase, but only to a certain point Vmax- maximum velocity At Vmax, the enzyme is working as fast as possible

Characteristics of enzyme active site

Catalytic site Where the reaction actually occurs Binding site Area that holds substrate in proper place Enzymes uses weak, non-covalent interactions to hold substrate in place based on R groups of amino acids Sites are pockets or cleft on the enzyme surface

Steps in an enzyme reaction

Enzyme and substrate combine to form a complex Complex goes through a transition state A complex of the enzyme and the product is produced The enzyme and product separate

Characteristic of enzyme active site Lock and key model Picture by Emil Fisher (1890) This model assumed that only a substrate of the proper shape could fit with the enzyme

Induced-fit model Proposed by Daniel Koshland (1958) This model assumes continuous changes in active site structure as a substrate binds This model recognizes that there is much flexibility in an enzymes structure According to this model, an enzyme is able to conform to a substrate

COFACTORS AND COENZYMES

A nonprotein component of enzymes is called the cofactor. Cofactors can be either organic or inorganic compounds .If the cofactor is organic, then it is called a coenzyme. Coenzymes are relatively small molecules compared to the protein part of the enzyme. Many of the coenzymes are derived from vitamins. The inorganic cofactors commonly are metal ions. (e.g. Ca, Cu, Co, Fe)

Enzymes that require a cofactor, but do not have one bound are called apoenzyme. An apoenzyme together with its cofactor(s) is called a holoenzyme (i.e., the active form)
COENZYME + SUBSTRATE APOENZYME + SUBSTRATE APOENZYME + COENZYME + SUBSTRATE NO PRODUCT NO PRODUCT PRODUCT

HOLOENZYME

Some vitamins that are often converted to coenzymes :

Vitamin
B1 (Thiamine) B2 (Riboflavin) B3 (Niacin)

Coenzyme
Thiamine pyrophosphate Flavin adenine dinucleotide (FAD)

Function
Decarboxylation Carries hydrogen

Nicotinamide Oxidation or adenine hydrogen transfer dinucleotide (NAD) Tetrahydrofolic acid Amino acid metabolism Coenzyme A Acyl group carrier

Folic acid Pantothenic acid

EFFECT OF pH & TEMPERATURE ON ENZYMATIC REACTIONS Exceeding normal pH and normal temperature ranges always reduces enzyme reactions rates Optimum temperature is usually 25-40C For pH, most enzymes work near pH 7

Temperature

pH

SPECIFIC ENZYME EXAMPLE

CHYMOTRYPSIN A proteolytic enzyme Digestion of dietary protein in small intestine Initially produced in an active form (zymogen) : chymotrypsinogen; and actived by tripsin Chymotripsin only works on amino acids containing an aromatic ring (phenylalanin, tyrosine, tryptophan)

CONCLUSION
ENZYME DEFENITION ENZYME NOMENCLATURE AND CLASSIFICATION ENZYME-SUBSTRATE INTERACTION COFACTOR AND COENZYME EFFECT OF pH TEMPERATURE

REFERENCES
Brownie AC, Kernohan JC. Biochemistry. A core text with self-assesment. Churchill Livingstone, 1999. Campbell PN, Smith AD. Biochemistry Illustrated 4th ed. Churchill Livingstone, 2000. Mathews CK, van Holde KE, Ahren KG. Biochemistry 3th ed, Addison-Wesley Publishing Company, 2000. Swaminathan R. Handbook of Clinical Biochemistry. New Delhi. Oxford University Press, 2004.