MODULATION OF THE ALLOSTERIC EQUILIBRIUM OF YEAST CHORISMATE MUTASE BY VARIATION OF A SINGLE AMINO-ACID RESIDUE

被引：14

作者：

GRAF, R ^{[1
]}

DUBAQUIE, Y ^{[1
]}

BRAUS, GH ^{[1
]}

机构：

[1] UNIV ERLANGEN NURNBERG, INST MIKROBIOL BIOCHEM & GENET, D-91058 ERLANGEN, GERMANY

来源：

JOURNAL OF BACTERIOLOGY | 1995年 / 177卷 / 06期

关键词：

D O I：

10.1128/jb.177.6.1645-1648.1995

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Chorismate mutase (EC 5.4.99.5) from the yeast Saccharomyces cerevisiae is an allosteric enzyme which can be locked in its active R (relaxed) state by a single threonine-to-isoleucine exchange at position 226. Seven new replacements of residue 226 reveal that this position is able to direct the enzyme's allosteric equilibrium, without interfering with the catalytic constant or the affinity for the activator.

引用

页码：1645 / 1648

页数：4

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