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pH对羧肽酶A结构和功能的影响：晶体学研究

Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies.

作者信息

Shoham G, Rees D C, Lipscomb W N

出版信息

Proc Natl Acad Sci U S A. 1984 Dec;81(24):7767-71. doi: 10.1073/pnas.81.24.7767.

DOI:10.1073/pnas.81.24.7767
PMID:6595659
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC392233/
Abstract

High-resolution crystal structures are described for carboxypeptidase A (EC 3.4.17.1) in crystals grown at pH 8.5, 9.0, and 9.5 and compared with the structure at pH 7.5. The comparison shows that in the pH range of 7.5-9.5 the enzyme structure is practically unchanged, and, most importantly, that the flexible side chain of Tyr-248 remains exclusively in the "up" position, away from the Zn atom, throughout the pH range. There is no evidence for binding of Tyr-248 to Zn at any of these pH values. We conclude that the interaction of Tyr-248 with Zn is not an essential part of the mechanism of carboxypeptidase A and that its occurrence is an artifact of chemical modification of Tyr-248. It is also suggested that Tyr-248 is not uniquely associated with the observed high pK of the enzymatic hydrolysis.

摘要

描述了在pH 8.5、9.0和9.5条件下生长的晶体中羧肽酶A（EC 3.4.17.1）的高分辨率晶体结构，并与pH 7.5时的结构进行了比较。比较结果表明，在7.5 - 9.5的pH范围内，酶的结构基本不变，最重要的是，在整个pH范围内，Tyr - 248的柔性侧链始终仅处于“向上”位置，远离锌原子。没有证据表明在这些pH值中的任何一个下Tyr - 248与锌结合。我们得出结论，Tyr - 248与锌的相互作用不是羧肽酶A作用机制的必要部分，其出现是Tyr - 248化学修饰的假象。还表明Tyr - 248与观察到的酶促水解的高pK值并非唯一相关。

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本文引用的文献

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Metallocarboxypeptidases: stability constants and enzymatic characteristics.金属羧肽酶：稳定常数与酶学特性
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Binding of ligands to the active site of carboxypeptidase A.配体与羧肽酶A活性位点的结合。
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8
Carboxypeptidase A mechanisms.羧肽酶A的作用机制。
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3875-8. doi: 10.1073/pnas.77.7.3875.
9
Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue.羧肽酶A与底物类似物之间的活性交换复合物的结构。
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10
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