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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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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.

  1. 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.
  2. Two kinds of cofactors, with examples Cofactors are broadly of three kinds; any two of these qualify as the answer:
  1. 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.
  2. 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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