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

EC NUMBER
COMMENTARY hide
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 hide
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+
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-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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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+
show the reaction diagram
UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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required as oxidant for NAD+ recycling, product of 2-oxoglutarate reduction is 2-hydroxyglutarate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.47 - 0.97
NAD+
0.0056 - 2.36
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
0.2 - 2.05
UDP-alpha-D-glucuronate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00031 - 0.0047
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
0.00015 - 0.0021
UDP-alpha-D-glucuronate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00028 - 0.26
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
7935
0.00075 - 0.001
UDP-alpha-D-glucuronate
995
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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coupled reaction of enzymes WbpB/WbpE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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coupled reaction of enzymes WbpB/WbpE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38271
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x * 38271, calculated for recombinant enzyme including His- and T7 tags
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 38271, calculated for recombinant enzyme including His- and T7 tags
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 3 months
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-20°C, stable for at least 3 weeks
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis