超冷水中羧肽酶Aα的结构与功能

Structure and function of carboxypeptidase A alpha in supercooled water.

作者信息

Thompson J S, Gehring H, Vallee B L

出版信息

Proc Natl Acad Sci U S A. 1980 Jan;77(1):132-6. doi: 10.1073/pnas.77.1.132.

DOI:10.1073/pnas.77.1.132

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC348222/

Abstract

The spectral and enzymatic characteristics of chromophoric derivatives of carboxypeptidase A alpha (EC 3.4.17.1) have been examined at subzero temperatures in supercooled water-in-oil emulsions. Substrate and temperature dependencies of enzyme kinetics indicated the existence of a solution-like enzyme phase that greatly extends the temperature range (greater than 60 degrees C) over which the activity of this enzyme can be measured. The emulsion spectra were virtually identical to those of solutions over a wide range of temperatures. Subzero temperatures (less than -10 degrees C) may induce changes of enzyme conformation but not of geometry at the site of the metal atom, nor do they adversely affect activity at any of the temperatures studied. Both structure and function of carboxypeptidase A alpha can be examined in supercooled water under identical reaction conditions.

摘要

在过冷水包油乳液中，于零下温度下研究了羧肽酶Aα（EC 3.4.17.1）发色衍生物的光谱和酶学特性。酶动力学对底物和温度的依赖性表明，存在一种类似溶液的酶相，极大地扩展了可测量该酶活性的温度范围（大于60摄氏度）。在很宽的温度范围内，乳液光谱与溶液光谱几乎相同。零下温度（低于-10摄氏度）可能会引起酶构象的变化，但不会改变金属原子位点的几何结构，在所研究的任何温度下也不会对活性产生不利影响。在相同反应条件下，可在过冷水中研究羧肽酶Aα的结构和功能。

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