To propose: A simple mechanism for the enzyme carboxypeptidase by referring to the classic paper of William Lipscomb. Introduction: Lipscomb paper start with an explanation of factors that impact the enzyme catalysis and discusses the entropy changes, transition state binding, chemical catalysis and other effects. Then he finds this the mechanism of catalysis of carboxypeptidase A. This clearly states that the entropy changes and responsible for substrate binding as the enzyme inhibit the rotational and translational degrees of freedom of the substrate after binding. Several charged amino acids and Zn 2 + compensation for the loss in entropy of the substrate by releasing water of solvation.

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Chapter 14, Problem 7P

Interpretation Introduction

To propose:

A simple mechanism for the enzyme carboxypeptidase by referring to the classic paper of William Lipscomb.

Introduction:

Lipscomb paper start with an explanation of factors that impact the enzyme catalysis and discusses the entropy changes, transition state binding, chemical catalysis and other effects. Then he finds this the mechanism of catalysis of carboxypeptidase A. This clearly states that the entropy changes and responsible for substrate binding as the enzyme inhibit the rotational and translational degrees of freedom of the substrate after binding. Several charged amino acids and Zn2+ compensation for the loss in entropy of the substrate by releasing water of solvation.

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