ENZYMES Apoenzyme - protein portion of the classified according to:

- hastens chemical reactions in organic enzyme - biochemical function

matter - Subject to denaturation, in which - substrate catalyzed
- catalyzes single or limited number of enzyme losses its activity - class of reaction catalyzed
chemical reactions - individual identification numbers
- large molecules confined in cells Holoenzyme - an active substance ex. AMS EC 3.2.1.1
- increase membrane permeability formed by combination of a co-enzyme
allows them to enter the blood and an apoenzyme. ENZYME ABBREVIATION IDENTIFICATIO
- measured in terms of their activity N NUMBER
Proenzyme or ZymogensAn inactive 1. Acid ACP 3.1.3.2
and not of their absolute values phosphatase
- appear in serum after cellular injury, enzyme precursor 2. Aldolase ALD 4.1.2.13
degradation of cells or from storage Eg. Coagulation factors and 3. Alkaline ALP 3.1.3.1
areas Digestive enzymes phosphatase
4. Amylase AMS 3.2.1.1
- used clinically as evidence of organ 5. Alanine ALT 2.6.1.2
damage Classification & Nomenclature aminotransfera
- specific for a substrate that it converts Oxidoreductases se
to a defined product Catalyze redox rxn. between 2 6. Aspartate AST 2.6.1.1
aminotransfera
substrates se
Function A-+ B →A + B- 7. Aldolase ALD 4.1.2.13
i. Hydration of CO2 (respiration) – E.g: Dehydrogenase (LD) 8. Angiotensin ACE 3.4.15.1
converting
Carbonic Anhydrase enzyme
ii. Nerve induction –Choline Transferases 9. Creatine CK 2.7.3.2
acetyltransferase (Cholinergic enzymes) Catalyze the transfer of a group kinase
iii. Muscle contraction -AChE between 2 substrates (A-X+ B →A + B- 10. True / ACHE 3.1.1.7
Acetyl
iv. Nutrient degradation (digestion): X)
cholinesterase
Pepsin, Amylase, Lipase Eg: Transferase (ALT, AST, GGT), Kinase 11. PCHE 3.1.1.8
v. Growth and reproduction: Helicase Pseudocholines
Hydrolases terase
(Cell division) 12. Gamma GGT 2.3.2.2
vi. Energy storage and use: LDH, PPK1 & Catalyze hydrolysis of various bonds glutamyl
PPK2 (Conversion and conservation of A–B + H2O→A–OH+ B–H transferase
ATP) Eg: Amylase (AMY), Lipase(LPS), 13. Glucose-6- G-6-PD 1.1.1.49
Phosphatase (ACP) phosphate
dehydrogenase
A. Components of an Enzyme 14. Lactic LD 1.1.1.27
Active Site - cavity of an enzyme Lyases dehydrogenase
where substrates bind and undergo a Removal of groups from substrates 15. Leukocyte LAP 3.4.11.1
alkaline
chemical reaction without hydrolysis; product remain
phosphatase
double bonds ATP → cAMP + PPi 16. Lipase LPS 3.1.1.3
Allosteric Site - cavity other than the Fructose biphosphate aldolase (ALS) 17. 5’N 3.1.3.5
5’Nucleotidase
active site that binds regulatory
molecules . Isomerases
. Interconversion of geometric, optical,
B. Terms associated with an enzyme or positional isomersA →B
Substrates - substances acted upon by . Triphosphate isomerase (TPI)
enzymes .
Specific for their particular enzyme . Isomerases
. Interconversion of geometric, optical or
Cofactors - substance added in the positional isomersA →B
enzyme substrate complex to manifest . Triphosphate isomerase (TPI)
the enzyme activity .
a. Coenzyme or Prosthetic group . Ligases
Organic: Nucleotide (NADP) &Vitamins . Joins 2 substrate molecules, coupled
b. Activator Inorganic: Metal ion (Cl, with breaking of pyrophosphate bond
Mg, Cu) in ATPAb + C →A–C + b
. Glutathione Synthetase (GSH-S)
Isoenzyme - similar enzymatic activity .
but differ in physical, biochemical, and ENZYME NOMENCLATURE
immunologic characteristics. standardized by Enzyme Commission
(EC) in 1961 and revised in 1972 and
1978