Information on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

for references in articles please use BRENDA:EC1.1.1.335
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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
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis
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Amino sugar and nucleotide sugar metabolism
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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
malfunction
physiological function
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
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
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-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
show the reaction diagram
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
0.00075 - 0.001
UDP-alpha-D-glucuronate
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
gene wbpB or PGN_0168, from mutant strain HG66, DNA and amino acid sequence determination and analysis, complementation of the wbpB-defective mutant strain by expression of wild-type gene wbpB
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis