Recall Using an energy diagram, show why the lock-and-key model could lead to an
ID: 1064230 • Letter: R
Question
Recall Using an energy diagram, show why the lock-and-key model could lead to an inefficient enzyme mechanism. Reflect and Apply Other things being equal, what is a potential disadvantage of an enzyme having a very high affinity for its substrate? Reflect and Apply Amino acids that are far apart in the amino acid sequence of an enzyme can be essential for its catalytic activity. What does this suggest about its active site? Reflect and Apply If only a few of the amino acid residues of a enzyme are involved in its catalytic activity, why does the need such a large number of amino acids? Reflect and Apply A chemist synthesizes a new compound may be structurally analogous to the transition-state species enzyme-catalyzed reaction. The compound is experimentally to inhibit the enzymatic reaction strongly. Is it likely that is indeed a transition-state analogue?Explanation / Answer
Ans 20.
The active site of the enzyme is the region where substrate molecule binds to enzyme and undergoes a chemical reaction. When amino acids that are far apart in amino acid sequence of enzymes are essential for catalytic activity of enzyme, they must form part of active site. For such situation these amino acids must come close to each other. Hence, the active site must be formed by amino acids by coming close to form a three dimensional structure due to folding of peptide chain in enzyme molecule.
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Ans 22.
Transition state analogues are chemical compounds having structure similar to transition state of substrate in enzyme catalyzed reaction. Transition state analogues bind more tightly to the enzyme than the actual substrate. Thus, they act as inhibitors in enzyme catalyzed reactions by blocking active site of enzyme.
Since, the compound synthesized by chemist is experimentally shown to inhibit the enzymatic reaction strongly. It is most likely that this compound is a transition state analogue.
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