This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
gene PGN_0002 is a wbpD homolog which is required for synthesis of UDP-ManNAc(3NAc)A. A PGN_0002-deficient mutant demonstrates an A-LPS biosynthesis deficiency, a pigmentless phenotype and reduced hemagglutination and gingipain activities on the cell surface compared with wild-type cells. PGN_0002 mutants are not immunoreactive to anti-A-LPS, and no HBP35 and Rgp diffuse bands are observed
gene PGN_0002 is a wbpD homolog which is required for synthesis of UDP-ManNAc(3NAc)A. A PGN_0002-deficient mutant demonstrates an A-LPS biosynthesis deficiency, a pigmentless phenotype and reduced hemagglutination and gingipain activities on the cell surface compared with wild-type cells. PGN_0002 mutants are not immunoreactive to anti-A-LPS, and no HBP35 and Rgp diffuse bands are observed
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. The enzyme complexed with acetyl-CoA and UDP is crystallized at pH 8.0 in the presence of 100 mM HEPPS, 16-20% (w/v) poly(ethylene glycol) 3400 and 210 mM tetramethylammonium chloride. The enzyme bound to CoA and UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate is crystallized using 17% (w/v) poly(ethylene glycol) 3400, 300 mM NaCl, 100 mM HEPPS (pH 8.0), 210 mM tetramethylammonium chloride
QM/MM calculations reveal two sequential steps in the catalyzation process. The nucleophilic attack of the C3-amino group of the substrate on the carbonyl carbon of acetyl-CoA occurs in concert with the departure of CoA from acetyl-CoA, generating a negatively charged CoA and a positively charged intermediate. Subsequently, the sulfur anion of CoA accepts the proton of the positively charged intermediate to yield the final product. Asn84 is important for promoting the catalysis by forming a hydrogen bond with the C3-amino group to position the lone pair of the electrons of the C3-amino group in an ideal orientation for nucleophilic attack and stabilize the transition states and intermediate
the enzymes WbpA, WbpB, WbpE, WbpD and WbpI which act stepwise manner starting from UDP-GlcNAc can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel
Evidence that WbpD is an N-acetyltransferase belonging to the hexapeptide acyltransferase superfamily and an important protein for O-antigen biosynthesis in Pseudomonas aeruginosa PAO1
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
Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1
Exploring the substrate-assisted acetylation mechanism by UDP-linked sugar N-acetyltransferase from QM/MM calculations: The role of residue Asn84 and the effects of starting geometries