Question of 41
Q.Non-protein constituents called co-factors are bound to the enzyme, to make it catalytically active.
(a) Name the protein part of the enzyme.
(b) Mention any two kinds of co-factors with examples.
(c) What happens to the catalytic activity of enzyme, when the co-factor is removed ?
Kerala DhseKerala DHSE Plus One Board 2021Subjective· 3mImportance★★★★★
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Start your 14-day free trial to unlock the full solution →Many enzymes are not pure protein; they need a small non-protein "helper" component (a cofactor) bound to the protein part before they can catalyse a reaction. Remove the cofactor and the protein alone cannot work.
An enzyme that requires a non-protein cofactor for activity is called a holoenzyme when complete (protein + cofactor together), and its two components are studied separately as follows.
- The protein part of the enzyme The protein component of such an enzyme is called the apoenzyme. By itself, the apoenzyme is catalytically inactive — it needs its cofactor to become a functional, active holoenzyme.
- Two kinds of cofactors, with examples Cofactors are broadly of three kinds; any two of these qualify as the answer:
- Prosthetic groups — organic cofactors that are tightly (often covalently) bound to the apoenzyme and remain permanently associated with it. Example: haem, which is a prosthetic group in the enzyme peroxidase (and in catalase), essential for the enzyme's catalytic action.
- Co-enzymes — organic cofactors that are only loosely/transiently bound and get attached to the enzyme just at the time of catalysis; many are derived from vitamins. Examples: NAD (nicotinamide adenine dinucleotide) and NADP (nicotinamide adenine dinucleotide phosphate), which act as coenzymes in many oxidation–reduction (dehydrogenase) reactions. …
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