2.6.1.98: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
This is an abbreviated version!
For detailed information about UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase, go to the full flat file.
Reaction
Synonyms
aminotransferase WbpE, PGN_1236, PorR, WbpE, WlbC, WpbE
ECTree
2.6.1.98 UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferaseAdvanced search results
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General Information on EC 2.6.1.98 - UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
malfunction
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B-band LPS production is restored to Pseudomonas aeruginosa knockout mutants when the relevant Bordetella pertussis genes are supplied in trans
metabolism
physiological function
additional information
metabolism
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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
metabolism
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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
metabolism
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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
metabolism
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
metabolism
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WbpE substrate 2-acetamido-2-deoxy-D-ribohex-3-uluronic acid is synthesized by WbpB
metabolism
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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metabolism
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the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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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
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 from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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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
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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physiological function
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WbpE from Pseudomonas aeruginosa catalyzes the amination of UDP-3-keto-2-acetamido-2-deoxy-D-glucuronic acid (UDP-3-keto-GlcNAcA) representing the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
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additional information
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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
additional information
WbpE nucleotide sugar-binding site structure, overview
additional information
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WbpE nucleotide sugar-binding site structure, overview
additional information
analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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additional information
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analysis of external aldimine structures of WpbE solved in the presence of either dTDP-3-amino-3,6-dideoxy-D-galactose or dTDP-3-amino-3,6-dideoxy-D-glucose
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