Catalytic mechanism of MraY and WecA, two paralogues of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily
Author:
Funder
CNRS
University of Paris Sud
European Community
Publisher
Elsevier BV
Subject
General Medicine,Biochemistry
Reference38 articles.
1. Modeling bacterial UDP-HexNAc: polyprenol-P HexNAc-1-P transferases;Price;Glycobiology,2005
2. The biosynthesis of peptidoglycan lipid-linked intermediates;Bouhss;FEMS Microbiol. Rev.,2008
3. Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis;Bouhss;J. Biol. Chem.,2004
4. Purification and characterization of the bacterial UDP-GlcNAc: undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA;Al-Dabbagh;J. Bacteriol.,2008
5. Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis;Al-Dabbagh;Biochemistry,2008
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