Orotidine 5′-Monophosphate Decarboxylase: Transition State Stabilization from Remote Protein-Phosphodianion Interactions

被引：37

作者：

Amyes, Tina L. ^{[1
]}

Ming, Shonoi A. ^{[1
]}

Goldman, Lawrence M. ^{[1
]}

Wood, B. McKay ^{[2
,3
]}

Desai, Bijoy J. ^{[2
,3
]}

Gerlt, John A. ^{[2
,3
]}

Richard, John P. ^{[1
]}

机构：

[1] SUNY Buffalo, Dept Chem, Buffalo, NY 14260 USA

[2] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[3] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 23期

基金：

美国国家卫生研究院;

关键词：

PROFICIENT ENZYME; CATALYSIS; ACTIVATION;

D O I：

10.1021/bi300585e

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：

Mutants of orotidine 5'-monophosphate decarboxylase containing all possible single (Q215A, Y217F, and R235A), double, and triple substitutions of the side chains that interact with the phosphodianion group of the substrate orotidine 5'-monophosphate have been prepared. Essentially the entire effect of these mutations on the decarboxylation of the truncated neutral substrate 1-(beta-D-erythrofuranosyl)orotic acid that lacks a phosphodianion group is expressed as a decrease in the third-order rate constant for activation by phosphite dianion. The results are consistent with a model in which phosphodianion binding interactions are utilized to stabilize a rare closed enzyme form that exhibits a high catalytic activity for decarboxylation.

引用

页码：4630 / 4632

页数：3

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[11] A PROFICIENT ENZYME [J].