QUESTION 4 Irreversible inhibitors: Decrease Vmax but do not alter Km O Decrease

Question

QUESTION 4 Irreversible inhibitors: Decrease Vmax but do not alter Km O Decrease Vmax and decrease Km Do not change Vmax but decrease Km Decrease Vmax and increase Km QUESTIONS Allosteric regulation refers to: Binding of an inhibitor to the active site that prevents binding of the substrate. Covalent modification of an amino acid in the active site of the enzyme. Proteolytic cleavage of a few of the N-terminal residues to activate the enzyme. Change in enzyme activity resulting from binding to a modulator that causes a conformational change in the enzyme. QUESTION 6 According to the steady state assumption, when the substrate is in excess (ie[J >>?ED the initial velocity equals Vmax because The interaction between the substrate and the enzyme is stronger. The rate of product formation is greater than the rate of ES formation. O The rate of ES formation equals the rate of ES breakdown. The affinity of the enzyme for the substrate is at maximum capacity.

Explanation / Answer

Answer 4: (a)-Decrease Vmax but do not alter Km.

Explanation:-Because Irreversible inhibitors decreas the Vmax value and their Km value clearly unchanged. Irreversible inhibitor can inhibit the enzymes activity permanently because they are Covalently altered the enzymes, that why they differ from other types of inhibitors.

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Answer 5: (d)-Change in enzyme activity resulting from binding to a modulator cause a conformational change in the enzyme.

Explanation: Allosteric regulation take place at a time at which a non-substrate molecule attach or altered a site other than the active site of an enzyme this site is known as allosteric site.So it prompting the enzymes to altered the shape. The altered shape can make the enzyme capable for action or inactivated.

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Answer 6: (c)- The rate of ES formation equals the rate of ES breakdown.

Explanation: When the Substrate concentration will greater than an enzyme concentration then all the active site of an enzyme occupied by the substrate .Thereby, they change Enzyme-Substrate complex and Vmax means the maximum enzyme activity at which all the enzyme are occupied in the substrate.

V= Vmax [S]/Km+S

When S> > > Km, at constant E, then neglecting Km, and cancelled the S by S, then remain only
V=Vmax

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