Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism

被引：20

作者：

Brewer, JM ^{[1
]}

Glover, CVC

Holland, MJ

Lebioda, L

机构：

[1] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA

[2] Univ Calif Davis, Dept Biol Chem, Sch Med, Davis, CA 95616 USA

[3] Univ S Carolina, Dept Chem & Biochem, Columbia, SC 29208 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1383卷 / 02期

关键词：

enolase; mutagenesis; catalytic mechanism; loop closure;

D O I：

10.1016/S0167-4838(98)00004-1

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 S39A mutant of yeast enolase (isozyme 1), prepared by site-directed mutagenesis, has a relative V-max of 0.01% and an activation constant for Mg2+ ca. 10-fold higher, compared with native enzyme. It is correctly folded. There is little effect of solvent viscosity on activity. We think that the loop Ser36-His43 fails to move to the 'closed' position upon catalytic Mg2+ binding, weakening several electrostatic interactions involved in the mechanism. (C) 1998 Elsevier Science B.V.

引用

页码：351 / 355

页数：5

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