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

McGlynn, Shawn E.Boyd, Eric S.Shepard, Eric M.Lange, Rachel K.Gerlach, RobinBroderick, Joan B.Peters, John W.2017-04-112017-04-112009-11McGlynn 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):595-5980021-9193https://scholarworks.montana.edu/handle/1/12699The 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.Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactorArticle