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Information on EC 1.1.1.136 - UDP-N-acetylglucosamine 6-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.136
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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
1.1.1.136 UDP-N-acetylglucosamine 6-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 expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
showSynonyms
udp-glcnac dehydrogenase, udp-n-acetylglucosamine 6-dehydrogenase, o180 o antigen, uglcnacdh, udp-glcnac 6-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, uridine diphosphoacetylglucosamine
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UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase
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UDP-GlcNAc dehydrogenase
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UDP-N-acetylglucosamine C-6 dehydrogenase
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UDPacetylglucosamine dehydrogenase
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uridine 5'-diphosphate-N-acetyl-D-glucosamine oxidoreductase
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uridine diphosphoacetylglucosamine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + 2 NADH + 2 H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis, UDP-N-acetyl-alpha-D-galactosaminuronate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:NAD+ 6-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.
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CAS REGISTRY NUMBER
COMMENTARY
9054-83-5
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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
UDP-D-glucose + NADP+
?
-
Substrates: at 10% the rate of UDP-N-acetyl-D-glucosamine and NAD+
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
UDP-N-acetyl-D-glucosamine + NADP+
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADPH
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Substrates: at 10% the rate of NAD+
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH
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Substrates: -
Products: product determination by NMR
Products: product determination by NMR
?
UDP-N-acetyl-D-glucosamine + NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH
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Substrates: the enzyme is involved in the biosynthesis of the Vi antigen, a clinically important vaccine antigen, in Salmonella typhi, pathway overview
Products: -
Products: -
?
additional information
?
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Substrates: no substrate: UDP-glucose, UDP-galactose, and UDP-N-acetylgalactosamine
Products: -
Products: -
?
additional information
?
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Substrates: no substrate: UDP-glucose, UDP-galactose, and UDP-N-acetylgalactosamine
Products: -
Products: -
?
additional information
?
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Substrates: determination of substrate specificity, no or poor activity with UDP-D-glucose, UDP-D-galactose, and UDP-D-galactosamine, overview
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-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
UDP-N-acetyl-D-glucosamine + NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH
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Substrates: the enzyme is involved in the biosynthesis of the Vi antigen, a clinically important vaccine antigen, in Salmonella typhi, pathway overview
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
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Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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tetramethylammonium, dimethylammonium or sodium slats do not substitute for NH4+ or K+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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positive cooperativity with respect to substrate binding, Hill coefficient 1.8
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0.276
NAD+
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pH 7.5, 25°C, recombinant enzyme
0.077
UDP-N-acetyl-D-glucosamine
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pH 7.5, 25°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.5
NAD+
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pH 7.5, 25°C, recombinant enzyme
15.5
UDP-N-acetyl-D-glucosamine
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pH 7.5, 25°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Achromobacter georgiopolitanum, wild-type and capsuleless mutant
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-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (1150 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.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120500
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recombinant enzyme, gel filtration
47675
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3 * 47675, subunit amino acid sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
trimer
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3 * 47675, subunit amino acid sequence calculation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate protects against inactivation during storage and incubation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified recombinant enzyme, in presence of 10 mM DTT, stable, even to multiple freeze-thaw cycles
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged TviB from Escherichia coli strain BL21(DE3) by two steps of anion exchange chromatography, affinity chromatography, and gel filtration, inactive oligomeric forms of the enzym eis removed in gel filtration, to near homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tviB located in the viaB locus, genetic organization, expression as C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawamura, T.; Ichihara, N.; Sugiyama, S.; Yokota, H.; Ishimoto, N.; Ito, E.
Biosynthesis of UDP-N-acetyl-D-glucosaminuronic acid and UDP-N-acetyl-D-mannosaminuronic acid in Micrococcus luteus
J. Biochem.
98
105-116
1985
Micrococcus luteus
brenda
Fan, D.F.; John, C.E.; Zalitis, J.; Feingold, D.S.
UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum
Arch. Biochem. Biophys.
135
45-49
1969
Alcaligenes sp.
brenda
Wheat, R.W.; Barrow, R.O.; Land, G.A.
Cellular localization of uridine 5-diphosphate-N-acetyl-D-glucosamine oxidoreductase activity in Citrobacter freundii
J. Bacteriol.
127
1032-1035
1976
Citrobacter freundii
brenda
Miller, W.L.; Wenzel, C.Q.; Daniels, C.; Larocque, S.; Brisson, J.R.; Lam, J.S.
Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1
J. Biol. Chem.
279
37551-37558
2004
Pseudomonas aeruginosa
brenda
Zhang, H.; Zhou, Y.; Bao, H.; Liu, H.W.
Vi antigen biosynthesis in Salmonella typhi: characterization of UDP-N-acetylglucosamine C-6 dehydrogenase (TviB) and UDP-N-acetylglucosaminuronic acid C-4 epimerase (TviC)
Biochemistry
45
8163-8173
2006
Salmonella enterica subsp. enterica serovar Typhi
brenda
Gu, X.; Glushka, J.; Lee, S.G.; Bar-Peled, M.
Biosynthesis of a new UDP-sugar, UDP-2-acetamido-2-deoxyxylose, in the human pathogen Bacillus cereus subspecies cytotoxis NVH 391-98
J. Biol. Chem.
285
24825-24833
2010
Bacillus cereus (A7GKX6), Bacillus cereus
brenda
Wang, Q.; Perepelov, A.V.; Beutin, L.; Senchenkova, S.N.; Xu, Y.; Shashkov, A.S.; Ding, P.; Knirel, Y.A.; Feng, L.
Structural and genetic characterization of the Escherichia coli O180 O antigen and identification of a UDP-GlcNAc 6-dehydrogenase
Glycobiology
22
1321-1331
2012
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.136)
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Release 2023.1 (January 2023)
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