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UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
additional information
?
-
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
transaminase WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
transaminase WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate. Cofactor pyridoxal 5'-phosphate is converted to pyridoxamine phosphate during the reaction
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
additional information
?
-
-
2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid WbpE product identification by mass spectrometry, overview
-
-
?
additional information
?
-
-
WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-N-acetyl-D-glucosaminuronate, UDP-GlcNAcA, to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate, UDP-GlcNAc(3NH2)A, in a coupled reaction via a unique NAD+ recycling pathway, large-scale coupled reaction WpbB/WpbE, overview. WbpA, WbpB, WbpE, WbpD and WbpI can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel. Addition of 0.2 mM NAD+, for WbpB, and 0.1 mM pyridoxal 5'-phosphate, for WbpE, to the reaction mixture aids in achieving complete turnover of substrate, which implies that the heterologously expressed proteins are not saturated with cofactor due to the limiting intracellular levels of both NAD+ and pyridoxal 5'-phosphate in Escherichia coli. WbpB/WbpE substrate specificity, overview
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-
?
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UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
transaminase WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
-
-
r
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
B-band LPS production is restored to Pseudomonas aeruginosa knockout mutants when the relevant Bordetella pertussis genes are supplied in trans
metabolism
-
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
-
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 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
-
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
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
metabolism
-
the enzyme catalyzes the third step in the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
additional information
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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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D156A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
H308A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
K185A
site-directed mutagenesis, the activity of the catalytic site mutant is completely abolished
N227A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
Q159A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
R229A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
S180A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
T60A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
Y309A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
additional information
-
construction of a nonpolar knockout of each of wbpA, wbpB, wbpE, wbpD, and wbpI genes. Expression of Bordetella pertussis genes wbpO1629 and wbpO3150 complements 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
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Westman, E.L.; Preston, A.; Field, R.A.; Lam, J.S.
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
J. Bacteriol.
190
6060-6069
2008
Bordetella pertussis, Pseudomonas aeruginosa
brenda
Larkin, A.; Olivier, N.B.; Imperiali, B.
Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly
Biochemistry
49
7227-7237
2010
Pseudomonas aeruginosa (Q9HZ76), Pseudomonas aeruginosa
brenda
Westman, E.L.; McNally, D.J.; Charchoglyan, A.; Brewer, D.; Field, R.A.; Lam, J.S.
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
J. Biol. Chem.
284
11854-11862
2009
Pseudomonas aeruginosa
brenda
Larkin, A.; Imperiali, B.
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
Biochemistry
48
5446-5455
2009
Pseudomonas aeruginosa
brenda
Shoji, M.; Sato, K.; Yukitake, H.; Naito, M.; Nakayama, K.
Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide
Sci. Rep.
4
5056
2014
Porphyromonas gingivalis (B2RK60), Porphyromonas gingivalis DSM 20709 (B2RK60)
brenda
Dow, G.T.; Gilbert, M.; Thoden, J.B.; Holden, H.M.
Structural investigation on WlaRG from Campylobacter jejuni A sugar aminotransferase
Protein Sci.
26
586-599
2017
Pseudomonas aeruginosa (Q9HZ76), Pseudomonas aeruginosa ATCC 15692 (Q9HZ76), Pseudomonas aeruginosa 1C (Q9HZ76), Pseudomonas aeruginosa PRS 101 (Q9HZ76), Pseudomonas aeruginosa DSM 22644 (Q9HZ76), Pseudomonas aeruginosa CIP 104116 (Q9HZ76), Pseudomonas aeruginosa LMG 12228 (Q9HZ76), Pseudomonas aeruginosa JCM 14847 (Q9HZ76)
brenda