| Literature DB >> 21335454 |
Susana Merino1, Natalia Jimenez, Raquel Molero, Lamiaa Bouamama, Miguel Regué, Juan M Tomás.
Abstract
The Aeromonas hydrophila AH-3 WecP represents a new class of UDP-HexNAc:polyprenol-P HexNAc-1-P transferases. These enzymes use a membrane-associated polyprenol phosphate acceptor (undecaprenyl phosphate [Und-P]) and a cytoplasmic UDP-d-N-acetylhexosamine sugar nucleotide as the donor substrate. Until now, all the WecA enzymes tested were able to transfer UDP-GlcNAc to the Und-P. In this study, we present in vitro and in vivo proofs that A. hydrophila AH-3 WecP transfers GalNAc to Und-P and is unable to transfer GlcNAc to the same enzyme substrate. The molecular topology of WecP is more similar to that of WbaP (UDP-Gal polyprenol-P transferase) than to that of WecA (UDP-GlcNAc polyprenol-P transferase). WecP is the first UDP-HexNAc:polyprenol-P GalNAc-1-P transferase described.Entities:
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Year: 2011 PMID: 21335454 PMCID: PMC3133024 DOI: 10.1128/JB.01441-10
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490