Any feedback?
Enzyme Nomenclature
Information on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.335Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenaseIUBMB Comments
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.
Specify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PGN_0168
WblA
WbpB
WlbA
WbpB
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
?
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+
-
-
-
-
?
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+
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
-
-
?
UDP-alpha-D-glucuronate + NAD+
UDP-alpha-D-ribo-hex-3-uluronate + NADH + H+
-
-
-
-
?
UDP-alpha-D-glucuronate + NAD+
UDP-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-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
-
-
?
additional information
?
-
-
the reaction mechanism is sequential, enzyme does not require 2-ketoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
-
-
?
additional information
?
-
the reaction mechanism is sequential, enzyme does not require 2-oxoglutarate for activity. No substrates: UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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+
-
-
-
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
required as oxidant for NAD+ recycling, product of 2-oxoglutarate reduction is 2-hydroxyglutarate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
presence of transaminase WlbC, 25°C, pH 8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please 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
-
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
-
Show AA Sequence and Transmembrane Helices (123 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38271
x * 38271, calculated for recombinant enzyme including His- and T7 tags
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 38271, calculated for recombinant enzyme including His- and T7 tags
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.335)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
