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Q.How is prosthetic group different from other co-factors? OR What will happen if the co-factor is removed from the enzyme?
Madhya Pradesh MpbseMP Board Higher Secondary (Class 11) 2026Subjective· 3mImportance★★★★★
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Start your 14-day free trial to unlock the full solution →Prosthetic groups are permanently and tightly bound to the enzyme, unlike other cofactors, which associate loosely and reversibly with the enzyme protein.
Many enzymes are conjugated proteins, requiring a non-protein component (a cofactor) in addition to the protein part (apoenzyme) to become catalytically active; the complete active enzyme (apoenzyme + cofactor) is called a holoenzyme. Cofactors can be broadly grouped as:
- Prosthetic groups — organic cofactors that are tightly and permanently attached to the enzyme protein, often by covalent bonds, and remain bound to the enzyme throughout its catalytic cycle (e.g. haem in catalase/peroxidase, or FAD in some oxidoreductases).
- Coenzymes — organic cofactors (often derived from vitamins, e.g. NAD+, NADP+, coenzyme A) that are only loosely and transiently associated with the enzyme; they bind to the enzyme just during the catalytic step, get chemically modified, and then dissociate to be regenerated elsewhere.
- Metal ion cofactors — inorganic ions (e.g. Zn2+, Mg2+) that may bind either tightly or loosely depending on the enzyme. …
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