Information on EC 1.1.1.136 - UDP-N-acetylglucosamine 6-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.136
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine 6-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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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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UDP-N-acetyl-alpha-D-galactosaminuronate biosynthesis
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Amino sugar and nucleotide sugar metabolism
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-83-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Achromobacter georgiopolitanum, wild-type and capsuleless mutant
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
ATCC 10053
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ATCC 4698
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Manually annotated by BRENDA team
ATCC 700931, gene tviB
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-D-glucose + NADP+
?
show the reaction diagram
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at 10% the rate of UDP-N-acetyl-D-glucosamine and NAD+
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?
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
UDP-N-acetyl-D-glucosamine + NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH
show the reaction diagram
UDP-N-acetyl-D-glucosamine + NADP+
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADPH
show the reaction diagram
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at 10% the rate of NAD+
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?
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-D-glucosamine + 2 NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
UDP-N-acetyl-D-glucosamine + NAD+ + H2O
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH
show the reaction diagram
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the enzyme is involved in the biosynthesis of the Vi antigen, a clinically important vaccine antigen, in Salmonella typhi, pathway overview
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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reduced at 10% the rate of NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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inhibition
Fe3+
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inhibition
Mn2+
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inhibition
NH4+
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enhancing activity
Ni2+
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inhibition
Zn2+
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inhibition
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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10 mM, more than 90% inhibition
N-acetylglucosamine 1-phosphate
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NADH
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competitive to NAD+
p-chloromercuribenzoate
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0.027 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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and the particulate fraction required for full activity
NH4+
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or K+, required
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 hide
LITERATURE
IMAGE
0.276 - 4.16
NAD+
0.077 - 0.84
UDP-N-acetyl-D-glucosamine
additional information
additional information
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positive cooperativity with respect to substrate binding, Hill coefficient 1.8
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.41 - 15.5
NAD+
0.97 - 15.5
UDP-N-acetyl-D-glucosamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
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above, Tris buffer
9
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glycine buffer
10
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above, glycine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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no activity above 50C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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isoelectric focusing
6
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predicted from gene sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50500
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calculated from cDNA
51500
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SDS-PAGE, His-tagged gnaA
120500
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recombinant enzyme, gel filtration
153000
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dynamic light scattering
162000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate protects against inactivation during storage and incubation
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monovalent cations protect against inactivation during incubation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 25% glycerol, stable for months
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-80C, purified recombinant enzyme, in presence of 10 mM DTT, stable, even to multiple freeze-thaw cycles
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4C, 1 M (NH4)2SO4, stable for more than 3 weeks
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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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recombinant protein with His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression in Escherichia coli
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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