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Enzyme Nomenclature
Information on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.335
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase
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 the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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enzyme WbpB is part of the B-band O-antigen pathway of Pseudomonas aeruginosa lipopolysaccharide. Proteins WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-GlcNAcA to UDP-GlcNAc(3NH2)A in a coupled reaction via a NAD+ recycling pathway
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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
2-acetamido-2-deoxy-alpha-D-glucuronic acid + NAD+ + L-glutamate
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid + NADH + 2-ketoglutarate
activity of enzyme His6-WbpB is detected only in presence of transaminase WbpE, and vice versa
product of the coupled reaction of enzyme WbpB and transaminase WbpE
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UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
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?
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
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?
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
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isolated enzyme EWbpB in presence of UDP-2-acetamido-2-deoxy-alpha-D-glucuronate and NAD+ does not show enzymic activity. Upon the addition of WbpE and L-glutamate to the reaction, complete turnover of the starting material and the formation of UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid are observed. No turnover is observed in the presence of UDP-N-acetyl-D-glucosamine or UDP-UDP-N-acetyl-D-galactosamine, and only minimal turnover is observed when UDP-D-glucuronic acid is used as the nucleotide sugar substrate. Enzyme WbpB prefers the glucopyranose configuration of the sugar as well as the presence of both the carboxylate at the C'' carbon and the acetylated amine at the C'' position. WbpE is specific for L-glutamate as the amine donor. Presence of 2-ketoglutarate is required as oxidant for NAD+ recycling
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UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
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UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
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additional information
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the reaction mechanism is sequential, enzyme does not require 2-ketoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
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additional information
?
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the reaction mechanism is sequential, enzyme does not require 2-oxoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
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required as oxidant for NAD+ recycling, product of 2-oxoglutarate reduction is 2-hydroxyglutarate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0056
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
presence of transaminase WlbC, 25°C, pH 8.5
0.015
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
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presence of transaminase WlbC, 25°C, pH 8.5
1.1
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
25°C, pH 8.5
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00031
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Chromobacterium violaceum
Q7NQL0
25°C, pH 8.5
0.00076
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Chromobacterium violaceum
Q7NQL0
presence of transaminase WlbC, 25°C, pH 8.5
0.0039
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Bordetella pertussis
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presence of transaminase WlbC, 25°C, pH 8.5
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00028
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Chromobacterium violaceum
Q7NQL0
25°C, pH 8.5
7935
0.136
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Chromobacterium violaceum
Q7NQL0
presence of transaminase WlbC, 25°C, pH 8.5
7935
0.26
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Bordetella pertussis
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presence of transaminase WlbC, 25°C, pH 8.5
7935
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 38271, calculated for recombinant enzyme including His- and T7 tags
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft
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crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis
in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
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in presence of NAD(H) and substrate to 2.13 A and 1.5 A resolution. Enzyme displays octameric quaternary structure with the active sites positioned far apart. The octamers can be envisioned as tetramers of dimers. The carboxylate group attached to the C-5' carbon of the hexose in the natural substrate, UDP-N-acetyl-D-glucosaminuronic acid, is held firmly in place in the enzyme WlbA active site by the side chains of Arg165 and Tyr169
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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synthesis of preparative quantities of 2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid and 2,3-diacetamido-2,3-dideoxy-D-glucuronic acid by coupled reaction of enzyme WbpB and transaminase WpbE
synthesis
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enzyme WbpB and the related enzymes of the B-band O-antigen pathway of Pseudomonas aeruginosa lipopolysaccharide, WbpA, WbpE, WbpD and WbpI, can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel, thereby providing supplies of this complex glycosyl donor for future studies of lipopolysaccharide assembly
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.335)
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