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Enzyme Nomenclature
Information on EC 2.6.1.98 - UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.6.1.98
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RECOMMENDED NAME
GeneOntology No.
UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate protein. 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. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335 (UDP-N-acetyl-2-amino-2-deoxyglucuronate oxidase).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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 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
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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
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
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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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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
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WbpE nucleotide sugar-binding site structure, overview
additional information
WbpE nucleotide sugar-binding site structure, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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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
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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
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-
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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
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transaminase WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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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
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WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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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
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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
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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
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r
additional information
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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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additional information
?
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2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid WbpE product identification by mass spectrometry, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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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
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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
Q9HZ76
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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
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transaminase WbpE product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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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
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WbpE/WlbC product is UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purifed recombinant detagged WbpE in complex with the cofactor pyridoxal 5'-phosphate and product UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid as the external aldimine, mixing of 0.0015 ml of protein solution containing 10 mg/ml protein in 25 mM HEPES, pH 8.0, 100 mM NaCl, 0.5% glycerol, and 0.5 mM UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid, with 0.0015 ml of reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate and 25% PEG 3350 for the wild-type enzyme, and 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium acetate, 10 mM SrCl2 and 25% PEG 3350 for the sselenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
precipitation occurs if the protein is left at ambient temperature or subjected to excessive freeze/thaw cycles
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged WpbE from Escherichia coli strain BL21-CodonPlus(DE3)RIL by nickel affinity chromatography
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recombinant His6-tagged WbpE from Escherichia coli strain Rosetta(DE3)
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recombinant N-terminal His6-tagged WbpE from Escherichia coli BL21-CodonPlus(DE3)RIL by nickel affinity chromatography, the N-terminal His6-tag is removed by proteolysis with TEV protease over the course of three days while stirring in dialysis buffer, followed by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene wbpE, expression of His6-tagged WbpE in Escherichia coli strain Rosetta(DE3)
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gene wbpE, expression of N-terminal His6-tagged WbpE in Escherichia coli BL21-CodonPlus(DE3)RIL
gene wbpE, expression of wild-type and mutants in Escherichia coli strain BL21(DE3)
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gene wlbC, i.e. wbpE, in Escherichia coli strain BL21(DE3), expression in wbpE knockout mutant of Pseudomonas aeruginosa PAO1 serotype O5
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gene wpbE, overexpression of N-terminally T7- and C-terminally His6-tagged WpbE in Escherichia coli strain BL21-CodonPlus(DE3)RIL
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.98)
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