<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Xu C</submitter><funding>NIAAA NIH HHS</funding><pagination>449-59</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3019819</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>193(2)</volume><pubmed_abstract>The O antigen is the outer part of the lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria and contains many repeats of an oligosaccharide unit. It contributes to antigenic variability and is essential to the full function and virulence of bacteria. Shigella is a Gram-negative human pathogen that causes diarrhea in humans. The O antigen of Shigella boydii type 14 consists of repeating oligosaccharide units with the structure [→6-d-Galpα1→4-d-GlcpAβ1→6-d-Galpβ1→4-d-Galpβ1→4-d-GlcpNAcβ1→]n. The wfeD gene in the O-antigen gene cluster of Shigella boydii type 14 was proposed to encode a galactosyltransferase (GalT) involved in O-antigen synthesis. We confirmed here that the wfeD gene product is a β4-GalT that synthesizes the Galβ1-4GlcNAcα-R linkage. WfeD was expressed in </pubmed_abstract><journal>Journal of bacteriology</journal><pubmed_title>Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis.</pubmed_title><pmcid>PMC3019819</pmcid><funding_grant_id>R01 AA020703</funding_grant_id><pubmed_authors>Allingham JS</pubmed_authors><pubmed_authors>Feng L</pubmed_authors><pubmed_authors>Szarek WA</pubmed_authors><pubmed_authors>Xu C</pubmed_authors><pubmed_authors>Liu B</pubmed_authors><pubmed_authors>Han Y</pubmed_authors><pubmed_authors>Hu B</pubmed_authors><pubmed_authors>Wang L</pubmed_authors><pubmed_authors>Brockhausen I</pubmed_authors></additional><is_claimable>false</is_claimable><name>Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis.</name><description>The O antigen is the outer part of the lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria and contains many repeats of an oligosaccharide unit. It contributes to antigenic variability and is essential to the full function and virulence of bacteria. Shigella is a Gram-negative human pathogen that causes diarrhea in humans. The O antigen of Shigella boydii type 14 consists of repeating oligosaccharide units with the structure [→6-d-Galpα1→4-d-GlcpAβ1→6-d-Galpβ1→4-d-Galpβ1→4-d-GlcpNAcβ1→]n. The wfeD gene in the O-antigen gene cluster of Shigella boydii type 14 was proposed to encode a galactosyltransferase (GalT) involved in O-antigen synthesis. We confirmed here that the wfeD gene product is a β4-GalT that synthesizes the Galβ1-4GlcNAcα-R linkage. WfeD was expressed in </description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Jan</publication><modification>2025-04-22T20:58:55.27Z</modification><creation>2019-03-27T00:38:02Z</creation></dates><accession>S-EPMC3019819</accession><cross_references><pubmed>21057010</pubmed><doi>10.1128/JB.00737-10</doi><doi>10.1128/jb.00737-10</doi></cross_references></HashMap>