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
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
收藏
页码:5357 / 5361
页数:5
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