4.4 Article

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

JOURNAL OF BACTERIOLOGY
Volume 192, Issue 2, Pages 595-598

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01125-09

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Funding

  1. NASA Astrobiology Institute (NAI)-Montana State University Astrobiology Biogeocatalysis Research Center [NNA08CN85A]
  2. Environmental and Biofilm Mass Spectrometry Facility through the Defense University Research Instrumentation Program (DURIP) [W911NF0510255]
  3. MSU program in Geobiological Systems [DGE 0654336]
  4. NAI

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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 CX3CX2C or CX2CX4C motif defining this family, HmdB contains a unique CX5CX2C motif.

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