Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor

Shawn E McGlynn; Eric S Boyd; Eric M Shepard; Rachel K Lange; Robin Gerlach; Joan B Broderick; John W Peters

doi:10.1128/JB.01125-09

Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor

J Bacteriol. 2010 Jan;192(2):595-8. doi: 10.1128/JB.01125-09. Epub 2009 Nov 6.

Authors

Shawn E McGlynn¹, Eric S Boyd, Eric M Shepard, Rachel K Lange, Robin Gerlach, Joan B Broderick, John W Peters

Affiliation

¹ Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.

Abstract

The genetic context, phylogeny, and biochemistry of a gene flanking the H(2)-forming methylene-H(4)-methanopterin dehydrogenase gene (hmdA), here designated hmdB, indicate that it is a new member of the radical S-adenosylmethionine enzyme superfamily. In contrast to the characteristic CX(3)CX(2)C or CX(2)CX(4)C motif defining this family, HmdB contains a unique CX(5)CX(2)C motif.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Motifs
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Catalytic Domain
Desulfitobacterium / enzymology
Desulfitobacterium / genetics
Hydrogenase / chemistry*
Hydrogenase / genetics
Hydrogenase / metabolism*
Methanococcus / enzymology
Methanococcus / genetics
Models, Molecular

Substances

Bacterial Proteins
Hydrogenase