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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
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
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
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
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
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
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.