S-Adenosyl-L-methionine:hydroxide adenosyltransferase:: A SAM enzyme

被引：22

作者：

Deng, Hai ^{[1
]}

Botting, Catherine H. ^{[1
]}

Hamilton, John T. G. ^{[2
]}

Russell, Rupert J. M. ^{[1
]}

O'Hagan, David ^{[1
]}

机构：

[1] Univ St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland

[2] Agri Food Biosci Inst, Agr Food & Environm Sci Div, Food Chem Branch, Belfast BT9 5PX, Antrim, North Ireland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 29期

基金：

英国生物技术与生命科学研究理事会;

关键词：

archaea; enzyme catalysis; fluorinase; nucleophilic substitution; SAM enzymes;

D O I：

10.1002/anie.200800794

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) Not so DUF: A DUF62 enzyme from the archaeon Pyrococcus horikoshii OT3 converts S-adenosyl-L-methionine (SAM) into adenosine through the nucleophilic attack of a hydroxide ion derived from water (see picture of the active site). The highly conserved nature of Asp68, Arg75, and His127 throughout the DUF62 protein superfamily suggests the wide-spread distribution of this novel catalytic activity in microorganisms. DUF = domain of unknown function. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5357 / 5361

页数：5

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