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.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

McGlynn SE,Boyd ES,Shepard EM,Lange RK,Gerlach R,Broderick JB,Peters JW

doi

10.1128/JB.01125-09

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

595-8

issue

2

eissn

0021-9193

issn

1098-5530

pii

JB.01125-09

journal_volume

192

pub_type

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