- Except for a small group of RNA molecules that act as catalyst, all enzymes are proteins.
- Catalytic activity of enzymes depends on the integrity of their native protein conformation.
- An enzyme loses its catalytic activity if it is denatured or dissociated into its subunits.
- The molecular weight of enzymes ranges from 12,000 to more than a million like other proteins.
- Some enzymes require no chemical groups for activity other than their amino acid residues, whereas others require additional chemical components called a co-factor.
- A co-factor may either be one or more inorganic ions or a complex organic or metallo-organic molecule called a co-enzyme.
- Some enzymes require both a co-enzyme and one or more metal ions for activity.
- The protein part of such enzyme is called apo-protein or apo-enzyme.
- A co-enzyme or metal ion that is very tightly or even covalently bound to the enzyme protein (apo-protein or apo-enzyme) is called a prosthetic group.
- A complete, catalytically active enzyme together with its bound co-enzyme and/or metal ions is called a holoenzyme.
- Enzyme proteins or apo-proteins are modified covalently by phosphorylation, glycosylation and other processes to regulate the enzyme activities.
Co-factor:
- A co-factor is a non-protein chemical substance or inorganic metallic ion that is required for the catalytic activity of an enzyme.
- There can be either one or more inorganic ions such as Fe2+, Mg 2+, Mn2+, Zn2+ etc. for the enzyme to properly act on the substrate.
- Some inorganic metal ions that serve as co-factors for the enzymes are given below.
S.N. | Ions | Enzymes |
1. | Cu2+ | Cytochrome oxidase |
2. | Fe2+ or Fe3+ | Cytochrome oxidase, catalase, peroxidase |
3. | K+ | Pyruvate kinase |
4. | Mg2+ | Hexokinase, glucose-6-phosphatase, pyruvate kinase |
5. | Mn2+ | Arginase, ribonucleotide reductase |
6. | Mo | Dinitrogenase |
7. | Ni2+ | Urease |
8. | Se | Glutathione peroxidase |
9. | Zn2+ | Carbonic anhydrase, alcohol dehydrogenase, carboxypeptidases A and B |
Co-enzyme:
- A co-enzyme is a complex non-protein organic or metallo-organic molecule that binds with an enzyme to catalyze a reaction.
- Co-enzymes act as transient carriers of specific functional groups.
- Most of the co-enzymes are derived from vitamins included in our diet.
- Some co-enzymes that serve as transient carries of specific atoms or functional groups are given below.
S.N | Co-enzyme | Chemical groups transferred | Dietary precursors in mammals |
1. | Biocytin | CO2 | Biotin |
2. | Co-enzyme A | Acyl groups | Pantothenic acid and other compounds |
3. | 5’-deoxyadenosylcobalamin (co-enzyme B12) | H atoms and alkyl groups | Vitamin B12 |
4. | Flavin adenine dinucleotide | Electrons | Riboflavin (vitamin B2) |
5. | Lipoate | Electrons and acyl groups | Not required in diet |
6. | Nocotinamide adenine dinucleotide (NAD) | Hydride ion (H–) | Nicotinic acid (Niacin) |
7. | Pyridoxal phosphate | Amino groups | Pyridoxine (vitamin B6) |
8. | Tetrahydrofolate | One-carbon groups | Folate or Folic acid |
9. | Thiamine pyrophosphate | Aldehydes | Thiamine (vitamin B1) |
International classification of enzymes:
- Many enzymes have been named by adding the suffix “ase” to the name of their substrate of to a word or phrase describing their activity.
- For example, urease catalyzes the hydrolysis of urea, and DNA polymerase catalyzes the polymerization of nucleotides to form DNA.
- The major groups of enzymes and the type of reaction they catalyze are given below.
Class No. | Class Name | Type of reaction catalyzed |
1. | Oxidoreductases | Transfer of electrons (hydride ions or H atoms) |
2. | Transferases | Group transfer reactions |
3. | Hydrolases | Hydrolysis of reactions (transfer of functional groups to water) |
4. | Lyases | Addition of groups to double bonds, or formation of double bonds by removal of groups |
5. | Isomerases | Transfer of groups within molecules to yield isomeric forms |
6. | Ligases | Formation of C-C, C-S, C-O, and C-N bonds by condensation reactions coupled to cleavage of ATP or similar co-factor |