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EC Number
General Information
WbpE is a member of the broad class of fold type I aspartate-aminotransferase enzymes, which harness the powerful electron-sink properties of PLP to carry out a wide variety of transformations, including transaminations, eliminations, decarboxylations, and racemizations. The general mechanism of this class of enzymes has been worked out in great detail, and is divided into two discrete half reactions that cycle between the PMP and PLP forms of the cofactor, overview
B-band LPS production is restored to Pseudomonas aeruginosa knockout mutants when the relevant Bordetella pertussis genes are supplied in trans
the biosynthetic pathway begins with WbpA, catalyzing the C6-oxidation of UDP-GlcNAc to give the corresponding UDP-N-acetyl-D-glucosaminuronic acid. The C3-dehydrogenase WbpB, aminotransferase WbpE, and acetyltransferase WbpD sequentially convert UDP-GlcNAcA into UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronic acid. Finally, the C2-epimerase WbpI modifies UDP-GlcNAc(3NAc)A to give the final UDP-ManNAc(3NAc)A
the biosynthetic pathway of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid production as part of the B-band LPS production requires the five enzymes WbpA, WbpB, WbpE, WbpD, and WbpI
the central carbohydrate of the Pseudomonas aeruginosa PAO1 (O5) B-band O-antigen, UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid or ManNAc(3NAc)A, is critical for virulence and is produced in a stepwise manner by the five enzymes in the Wbp pathway, WbpA, WbpB, WbpE, WbpD and WbpI, overview
WbpE substrate 2-acetamido-2-deoxy-D-ribohex-3-uluronic acid is synthesized by WbpB
Bordetella pertussis genes wbpO1629 and wbpO3150 complement a wbpA knockout of Pseudomonas aeruginosa. B-band LPS production is restored to Pseudomonas aeruginosa knockout mutants when the relevant Bordetella pertussis genes are supplied in trans
WbpE nucleotide sugar-binding site structure, overview
physiological function
a strain lacking PorR activity expresses the conventional O-antigen of orphyromonas gingivalis strain W50 (O-LPS), but lacks A-LPS, i.e. a different O-antigen consisting of an anionic polysaccharide (APS) repeat unit. PorE is a homolog of WbpE
physiological function
WbpE, a nucleotide sugar aminotransferase involved in O-antigen assembly, is a pyridoxal 5'-phosphate-dependent aminotransferse responsible for the conversion of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid and L-glutamate to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid and 2-oxoglutarate, respectively
Results 1 - 10 of 10