From hyperthermophiles to psychrophiles: the structural basis of temperature stability of the amino acid dehydrogenases

被引：8

作者：

Baker, PJ ^{[1
]}

机构：

[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2004年 / 32卷

关键词：

alanine dehydrogenase; glutamate dehydrogenase; maltosyltransferase; phosphoglucose isomerase; structure;

D O I：

10.1042/BST0320264

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The determination and comparison of the structures of a number of glutamate dehydrogenases that span the spectrum of thermal stability from mesophiles to hyperthermophiles have revealed that the formation of extended ion-pair networks is a major stabilizing feature in the adaptation of the organism to life at 100degreesC. Analysis of the structures of other hyperthermophilic proteins has shown that ion-pair networks also play roles in their stabilization, including the phosphoglucose isomerase from Pyrococcus furiosus and the maltosyltransferase from Thermotoga moritima.

引用

页码：264 / 268

页数：5

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