S-Adenosyl-L-methionine:Hydroxide Adenosyltransferase: A SAM Enzyme

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...

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Published inAngewandte Chemie (International ed.) Vol. 47; no. 29; pp. 5357 - 5361
Main Authors Deng, Hai, Botting, Catherine H, Hamilton, John T.G, Russell, Rupert J.M, O'Hagan, David
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 07.07.2008
WILEY-VCH Verlag
WILEY‐VCH Verlag
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Summary: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.
Bibliography:http://dx.doi.org/10.1002/anie.200800794
This research is supported by the Biotechnological and Biological Science Research Council. We thank Dr. K. Fujita from NBRC (NITE-DOB, Japan) for providing the clone containing ORF PH0463. We thank the BBSRC for a research grant and the Wellcome Trust for mass-spectrometry support. SAM=S-adenosyl-L-methionine.
NBRC
ark:/67375/WNG-6X1VJN6H-P
Biotechnological and Biological Science Research Council
istex:900F9EB1217D0968839AFB03DB1C362FF041599C
ArticleID:ANIE200800794
This research is supported by the Biotechnological and Biological Science Research Council. We thank Dr. K. Fujita from NBRC (NITE‐DOB, Japan) for providing the clone containing ORF PH0463. We thank the BBSRC for a research grant and the Wellcome Trust for mass‐spectrometry support. SAM=
S
L
methionine.
adenosyl
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200800794