Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1.
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Purified WbpA is a UDP-GlcNAc 6-dehydrogenase that uses NAD+.
"the data revealed that WbpA is a UDP-N-acetyl-D-glucosamine 6-dehydrogenase (EC 1.1.1.136), which uses NAD(+) as a coenzyme"
Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters.
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wbpA knockout lacks B-band O antigen.
"The wbpA knockout of P. aeruginosa PAO1 is devoid of B-band O antigen but still produces A-band O antigen in a variety of lengths."
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The dehydrogenase assays in this paper were on the B. pertussis WbpO enzymes, not WbpA.
"Capillary electrophoresis was used to characterize the enzymatic activities of purified WbpO(1629) and WbpO(3150)"
Pseudomonas aeruginosa B-band lipopolysaccharide genes wbpA and wbpI and their Escherichia coli homologues wecC and wecB are not functionally interchangeable.
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods