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1.1.1.335
malfunction
mutants porR and porT are involved in the pigmentation phenotype in Porphyromonas gingivalis. Porphyromonas gingivalis has two different lipopolysaccharide (LPS) molecules, O-LPS and A-LPS. Porphyromonas gingivalis strain HG66 lacks lipopolysaccharide A-LPS. Introduction of a wild-type wbpB gene into strain HG66 restores formation of A-LPS. Sequencing of the wbpB gene from strain HG66 has revealed the presence of a nonsense mutation in the gene, the porR mutation. The porR mutant possesses O-LPS, but lacks A-LPS
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743790
1.1.1.335
physiological function
A-LPS consists of a lipid A-core and anionic polysaccharide (APS) repeating units containing phosphorylated branched mannan. The PorR, WbpB and UgdA proteins are predicted to participate in the initial synthesis of structural sugar(s) in the anionic polysaccharide
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743790
1.1.1.335
physiological function
enzyme WbpB is part of the B-band O-antigen pathway of Pseudomonas aeruginosa lipopolysaccharide. Proteins WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-GlcNAcA to UDP-GlcNAc(3NH2)A in a coupled reaction via a NAD+ recycling pathway
718852
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