Co-factor

cofactor enzyme apoenzyme haloenzyme prosthetic group metal ion coenzyme

1. Co-Factor

2. Co-Factor Apoenzyme Protein Enzyme

3. Cofactors are non protein molecules that assist enzyme during that Catalysis of reactions . Enzyme without its cofactor is referred to as an apoenzyme The complete, catalytically active enzyme is called holoenzyme

4. Cofactor can be subdivided into three groups

5. Prosthetic group The organic compound which are tightly bind the cofactors are called prosthetic group Loosely bound cofactors serve functions like those of prosthetic group but bind in a transient, disposable manner either to the enzyme or to a substrate They are more likely substrate because they bind to and are released from the enzyme just as substrate and products are formed

6. Prosthetic group Tightly integrated into the enzyme structure by covalent or non covalent force B ) Inorganic Metal are the most common prosthetic group Metal ions : Cobalt , copper,Magnesium , Manage, Zinc, iron A) organic Flavin mononucleotide Flavin adenine dinucleotide Biotin Continue....

7. Enzyme that contain tightly bound metal ion are termed- metalloenzyme enzyme that require metal ion as loosely bound cofactor are termed as metal activated enzyme Metal ion facilitate binding and orientation of the substrate Formation of covalent bond with reaction intermediates Interact with substrate to render them more electrophilic and nucleophilic Role of metal ions

8. Coenzymes serve as a recyclable shuttles - or group - transfer agent that transport many substrates from their point of generation to their point of utilisation. Nicotinamide is a component of the redox coenzyme NAD and NADP Riboflavin is a component of the redox coenzyme FMN and FAD Thiamin participate in decarboxylation of α - ketogluteric acids and folic acid Coenzymes

9. Hydrogen atom or hydride ions Methyl group Acyl group Oligosaccharide Continue.... Chemical materials transported by coenzyme include