NDLI: 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.

Content Provider	Semantic Scholar
Author	McGlynn, Shawn E. Boyd, Eric S. Shepard, Eric M. Lange, Rachel K. Gerlach, Robin Broderick, Joan B. Peters, John W.
Copyright Year	2010
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.
Starting Page	129
Ending Page	129
Page Count	1
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.chemistry.montana.edu/jbroderick/publications/documents/J%20Bacteriol%202010%20McGlynn.pdf
Alternate Webpage(s)	https://scholarworks.montana.edu/xmlui/bitstream/handle/1/12699/10-017_Identification_and_characterization.pdf?isAllowed=y&sequence=1
PubMed reference number	19897660v1
Alternate Webpage(s)	https://doi.org/10.1128/JB.01125-09
DOI	10.1128/jb.01125-09
Journal	Journal of bacteriology
Volume Number	192
Issue Number	2
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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