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.
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.
McGlynn
Shawn E
SE
Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.
Boyd
Eric S
ES
Shepard
Eric M
EM
Lange
Rachel K
RK
Gerlach
Robin
R
Broderick
Joan B
JB
Peters
John W
JW
D020816:Amino Acid Motifs; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D045858:Desulfitobacterium / Q000201:enzymology / Q000235:genetics; D006864:Hydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017017:Methanococcus / Q000201:enzymology / Q000235:genetics; D008958:Models, Molecular
D001426:Bacterial Proteins; D006864:Hydrogenase