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
Date
2009-11Author
McGlynn, Shawn E.
Boyd, Eric S.
Shepard, Eric M.
Lange, Rachel K.
Gerlach, Robin
Metadata
Show full item recordAbstract
The genetic context, phylogeny, and biochemistry of a gene flanking the H2-forming methylene-H4-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 CX3CX2C or CX2CX4C motif defining this family, HmdB contains a unique CX5CX2C motif.
Citation
McGlynn SE, Boyd ES, Shepard EM, Lange R, Gerlach R, Broderick JB, Peters JW, "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," Journal of Bacteriology 2010 192(2):595-598