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

EC NUMBER
COMMENTARY hide
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 hide
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
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene wlbC
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant His6-tagged WbpE, 3 weeks, stable
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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
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 hide
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