Structure-function relationships of glutamine synthetases

被引：302

作者：

Eisenberg, D

Gill, HS

Pfluegl, GMU

Rotstein, SH

机构：

[1] Univ Calif Los Angeles, US DOE, Lab Struct Biol & Mol Med, Dept Chem, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, US DOE, Lab Struct Biol & Mol Med, Dept Biochem, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, US DOE, Lab Struct Biol & Mol Med, Dept Biol Chem, Los Angeles, CA 90095 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1477卷 / 1-2期

基金：

美国国家卫生研究院;

关键词：

glutamine synthetase; kinetic study; feedback inhibition; structural study; mechanism of action;

D O I：

10.1016/S0167-4838(99)00270-8

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：

As a highly regulated enzyme at the core of nitrogen metabolism, glutamine synthetase has been studied intensively. We review structural and functional studies of both bacterial and eukaryotic glutamine synthetases, with emphasis on enzymatic inhibitors. (C) 2000 Elsevier Science B.V. All rights reserved.

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页码：122 / 145

页数：24

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