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 in | Angewandte Chemie (International ed.) Vol. 47; no. 29; pp. 5357 - 5361 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
Wiley-VCH Verlag
07.07.2008
WILEY-VCH Verlag WILEY‐VCH Verlag |
Subjects | |
Online Access | Get full text |
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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. |
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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 |