Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5′-monophosphate decarboxylase:: A two-part substrate approach

被引：36

作者：

Barnett, Shonoi A. ^{[1
]}

Amyes, Tina L. ^{[1
]}

Wood, Bryant M. ^{[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 | 2008年 / 47卷 / 30期

关键词：

D O I：

10.1021/bi800939k

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：

Kinetic analysis of decarboxylation catalyzed by S154A, Q215A, and S154A/Q215A mutant yeast orotidine 5'-monophosphate decarboxylases with orotidine 5'-monophosphate (OMP) and with a truncated nucleoside substrate (EO) activated by phosphite dianion shows (1) the side chain of Ser-154 stabilizes the transition state through interactions with the pyrimidine rings of OMP or EO, (2) the side chain of Gln-215 interacts with the phosphodianion group of OMP or with phosphite dianion, and (3) the interloop hydrogen bond between the side chains of Ser-154 and Gln-215 orients the amide side chain of Gln-215 to interact with the phosphodianion group of OMP or with phosphite dianion.

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页码：7785 / 7787

页数：3

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