Question 21 1. Phenylmethane-sulfonyl-fluoride (PMsF inactivates serine protease

Question

Question 21 1. Phenylmethane-sulfonyl-fluoride (PMsF inactivates serine proteases covalently to the by binding by the catalytic serine residue at the active site: this enzyme-inhibitor bond is cleaved not enzyme. This is an example of what kind of inhibition? A. Non-competitive B. Competitive C. Irreversible D. pH inhibition E. Mixed 3 points Question 22 1. The role of the metal ion (Mg2)in catalysis by enolase lsto: A. act as a general base catalyst. B. stabilize protein conformation. C. facilitate general acid catalysis. D, facilitate general base catalysis. E. act as a general acid catalyst. 3 points Question 23 control of enzymatic activity is false? 1. Which of the following satements about allosteric several subunits. A. Allosteric proteins are generally composed of B. An effector may either inhibit or activate an enzyme. plots. C Allosteric effectors give rise to sigmoidal Wo vs [Sl kinetic D. Hererotropic allosteric effectors compete with substrate for binding sites. E. Binding of the effector changes the conformation of the enzyme molecule. points Question 24 binding to asite other than the 1. A small molecule that decreases the activity of an enzyme by catalytic site is termed a(n): A. competitive inhibitor. B. transition-state analog. allosteric inhibitor. c. D. alternative inhibitor. E. stereospecific agent. points 3

Explanation / Answer

Ans. 21 C irreversible

Phenyl methyl sulfonyl fluoride PMSF binds irreversibly with serine proteases , by forming a covalent bond and inactivates it . this inhibits the activitiy of enzyme irresponsibly

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