<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>193(8)</volume><submitter>Merino S</submitter><pubmed_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.</pubmed_abstract><journal>Journal of bacteriology</journal><pagination>1943-52</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3133024</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family.</pubmed_title><pmcid>PMC3133024</pmcid><pubmed_authors>Merino S</pubmed_authors><pubmed_authors>Molero R</pubmed_authors><pubmed_authors>Bouamama L</pubmed_authors><pubmed_authors>Jimenez N</pubmed_authors><pubmed_authors>Regue M</pubmed_authors><pubmed_authors>Tomas JM</pubmed_authors></additional><is_claimable>false</is_claimable><name>A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family.</name><description>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.</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Apr</publication><modification>2026-05-04T02:24:05.583Z</modification><creation>2019-03-27T03:06:54Z</creation></dates><accession>S-EPMC3133024</accession><cross_references><pubmed>21335454</pubmed><doi>10.1128/JB.01441-10</doi><doi>10.1128/jb.01441-10</doi></cross_references></HashMap>