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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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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
IUBMB Comments
This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.1.1.335
-
retroviral
-
capsid
-
retroviruses
- trim5alpha
-
rhesus
-
tripartite
- cyclophilin
-
antiretroviral
-
simian
-
macaque
-
trimcyps
-
anti-hiv-1
-
trim5-cyclophilin
-
indian-origin
-
post-entry
-
sivmac239
- trim22
-
spry
-
alpha-mediated
- synthesis
Reaction Schemes
showSynonyms
PGN_0168, WblA, WbpB, WlbA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PGN_0168
WblA
WbpB
WlbA
WbpB
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-
-
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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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-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: activity of enzyme His6-WbpB is detected only in presence of transaminase WbpE, and vice versa
Products: product of the coupled reaction of enzyme WbpB and transaminase WbpE
Products: product of the coupled reaction of enzyme WbpB and transaminase WbpE
?
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 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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Substrates: -
Products: -
Products: -
?
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
Substrates: -
Products: -
Products: -
?
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+
Substrates: 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
Products: -
Products: -
?
UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
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Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
additional information
?
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-
Substrates: the reaction mechanism is sequential, enzyme does not require 2-ketoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
Products: -
Products: -
?
additional information
?
-
Substrates: the reaction mechanism is sequential, enzyme does not require 2-oxoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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+
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
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
-
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
25°C, pH 8.5
0.00076
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
presence of transaminase WlbC, 25°C, pH 8.5
0.0039
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
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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
25°C, pH 8.5
0.136
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
presence of transaminase WlbC, 25°C, pH 8.5
0.26
UDP-2-acetamido-2-deoxy-alpha-D-glucuronate
-
presence of transaminase WlbC, 25°C, pH 8.5
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
mutants porR and porT are involved in the pigmentation phenotype in Porphyromonas gingivalis. Porphyromonas gingivalis has two different lipopolysaccharide (LPS) molecules, O-LPS and A-LPS. Porphyromonas gingivalis strain HG66 lacks lipopolysaccharide A-LPS. Introduction of a wild-type wbpB gene into strain HG66 restores formation of A-LPS. Sequencing of the wbpB gene from strain HG66 has revealed the presence of a nonsense mutation in the gene, the porR mutation. The porR mutant possesses O-LPS, but lacks A-LPS
malfunction
-
mutants porR and porT are involved in the pigmentation phenotype in Porphyromonas gingivalis. Porphyromonas gingivalis has two different lipopolysaccharide (LPS) molecules, O-LPS and A-LPS. Porphyromonas gingivalis strain HG66 lacks lipopolysaccharide A-LPS. Introduction of a wild-type wbpB gene into strain HG66 restores formation of A-LPS. Sequencing of the wbpB gene from strain HG66 has revealed the presence of a nonsense mutation in the gene, the porR mutation. The porR mutant possesses O-LPS, but lacks A-LPS
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physiological function
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
physiological function
A-LPS consists of a lipid A-core and anionic polysaccharide (APS) repeating units containing phosphorylated branched mannan. The PorR, WbpB and UgdA proteins are predicted to participate in the initial synthesis of structural sugar(s) in the anionic polysaccharide
physiological function
-
A-LPS consists of a lipid A-core and anionic polysaccharide (APS) repeating units containing phosphorylated branched mannan. The PorR, WbpB and UgdA proteins are predicted to participate in the initial synthesis of structural sugar(s) in the anionic polysaccharide
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Show AA Sequence and Transmembrane Helices (123 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38271
x * 38271, calculated for recombinant enzyme including His- and T7 tags
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
detection nonsense mutation in the gene wbpB from strain HG66 by sequencing. Porphyromonas gingivalis strain HG66 lacks lipopolysaccharide A-LPS. Introduction of a wild-type wbpB gene into strain HG66 restores formation of A-LPS. Presence of a nonsense mutation in the gene, the porR mutation. The porR mutant possesses O-LPS, but lacks A-LPS
additional information
-
detection nonsense mutation in the gene wbpB from strain HG66 by sequencing. Porphyromonas gingivalis strain HG66 lacks lipopolysaccharide A-LPS. Introduction of a wild-type wbpB gene into strain HG66 restores formation of A-LPS. Presence of a nonsense mutation in the gene, the porR mutation. The porR mutant possesses O-LPS, but lacks A-LPS
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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
synthesis
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Westman, E.L.; McNally, D.J.; Charchoglyan, A.; Brewer, D.; Field, R.A.; Lam, J.S.
Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa
J. Biol. Chem.
284
11854-11862
2009
Pseudomonas aeruginosa (G3XD23)
brenda
Larkin, A.; Imperiali, B.
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1
Biochemistry
48
5446-5455
2009
Pseudomonas aeruginosa (G3XD23)
brenda
Thoden, J.; Holden, H.
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
Biochemistry
49
7939-7948
2010
Pseudomonas aeruginosa (G3XD23), Thermus thermophilus (Q72KX8)
brenda
Thoden, J.; Holden, H.
Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
Biochemistry
50
1483-1491
2011
Bordetella pertussis, Chromobacterium violaceum (Q7NQL0)
brenda
Shoji, M.; Sato, K.; Yukitake, H.; Naito, M.; Nakayama, K.
Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide
Sci. Rep.
4
5056
2014
Porphyromonas gingivalis (B2RH42), Porphyromonas gingivalis DSM 20709 (B2RH42)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.335)
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Release 2023.1 (January 2023)
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