Q. Allosteric enzymes consist of multiple

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Q. The nonsubstrate molecules that binds to the allosteric sites are called as

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Q. Competitive inhibitors and real substrate often have similar

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Q. Competitive inhibition can be overcome by using

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Q. In competitive inhibition, the two things that binds to enzyme active site are

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Q. Enzyme-catalyzed modifications are

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Q. Covalent modification is means of changing

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Q. Irreversible modifications require the synthesis of

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Q. Enzyme which helps in changing the shape of molecule is called

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Q. Transmethylases helps in transfer of

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Q. Ligases helps in the

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Q. The enzyme involved in splitting or formation of C-C bond is called

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Q. Enzymes which are involved in transfer of electrons are

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Q. While bound to the active site, the substrate is converted into the

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Q. The enzyme increases the rate of reaction by

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Q. Enzymes do not change the

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Q. The substrate binds to specific region of enzyme called

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Q. Catalysts that increase the rate of biological chemical reaction are called as

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Q. In enzyme catalytic reaction the substrate is first converted to a high energy state called

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Q. The equilibrium constant is related to Gibb's free energy change for the reaction as

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