Information on EC 5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.1.3.7
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine 4-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Metabolic pathways
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teichuronic acid biosynthesis (B. subtilis 168)
-
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UDP-N-acetyl-D-galactosamine biosynthesis I
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UDP-N-acetyl-D-galactosamine biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine 4-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-16-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 168/W23, and 4 mutants carrying a gneA marker devoid of epimerase activity
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-
Manually annotated by BRENDA team
NCTC 11168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene GNE
-
-
Manually annotated by BRENDA team
gene gne2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
LY03 and Sfi20
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
biotype 2 serovar E, isoform Gne
UniProt
Manually annotated by BRENDA team
galE-like gene gne in the OPS gene cluster, and gene galE in the gal operon
-
-
Manually annotated by BRENDA team
galE-like gene gne in the OPS gene cluster, and gene galE in the gal operon
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-
Manually annotated by BRENDA team
genes gne1 and gne2
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-
Manually annotated by BRENDA team
genes gne1 and gne2
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
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
UDP-D-galactose
show the reaction diagram
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
show the reaction diagram
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
show the reaction diagram
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
show the reaction diagram
-
-
-
r
additional information
?
-
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-D-glucose
UDP-D-galactose
show the reaction diagram
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the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
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-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
show the reaction diagram
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
show the reaction diagram
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
show the reaction diagram
Q868I5
-
-
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r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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stimulates to a lesser degree than NAD+
NADPH
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stimulates to a lesser degree than NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
stimulates
Co2+
-
stimulates
Mn2+
-
stimulates
additional information
-
activity is independent of divalent metal
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-Bromo-2-hydroxy-naphthalene-1-carbaldehyde O-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-oxime
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IC50: 0.025 mM, specific for UDP-GlcNAc 4-epimerase, powerful reagent for reversible inhibition of O-linked glycosylation
glucosamine
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competitive with UDP-N-acetylglucosamine
iodoacetate
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Mg2+
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slight inhibition at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-[2-(Diethylamino)ethyl]amino-5,11-dihydro[1]benzoxepino[3,4-b]pyridine trihydrochloride
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 0.784
UDP-D-galactose
0.153 - 0.78
UDP-D-glucose
0.85
UDP-GalNAc
Vmax 1.02 mM/min
1.22
UDP-GlcNAc
Vmax 0.59 mM/min
0.519 - 0.887
UDP-N-acetyl-alpha-D-glucosamine
0.131 - 1.07
UDP-N-acetyl-D-galactosamine
0.137 - 1.087
UDP-N-acetyl-D-glucosamine
0.0114
UDP-N-acetylgalactosamine
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-
0.0011 - 4.4
UDP-N-acetylglucosamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4 - 290.1
UDP-D-galactose
0.52 - 73.95
UDP-D-glucose
0.58 - 1
UDP-N-acetyl-alpha-D-glucosamine
247.9
UDP-N-acetyl-D-galactosamine
Campylobacter jejuni
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MalE-Gne fusion protein
82.3 - 62300
UDP-N-acetyl-D-glucosamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.93 - 1.73
UDP-N-acetyl-alpha-D-glucosamine
1424
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
6-Bromo-2-hydroxy-naphthalene-1-carbaldehyde O-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-oxime
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
6-Bromo-2-hydroxy-naphthalene-1-carbaldehyde O-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-oxime
Homo sapiens
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IC50: 0.025 mM, specific for UDP-GlcNAc 4-epimerase, powerful reagent for reversible inhibition of O-linked glycosylation
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0119
growth on D-galactose as sole carbon source
0.0206
growth on D-glucose as sole carbon source
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.6
substrate UDP-GlcNAc
8
-
assay at
8 - 8.5
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8 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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over 50% of maximal activity at pH 6.0 and pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
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without NAD+
40 - 45
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in presence of 1 mM NAD+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
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20% of maximal activity at 10°C and at 50°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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embryonic
Manually annotated by BRENDA team
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ldlD cells are deficient in UDP-N-acetylglucosamine 4-epimerase
Manually annotated by BRENDA team
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activity increases after transient mild inflammation produced by the subcutaneous injection of either carageenan or monosodium urate crystals
Manually annotated by BRENDA team
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UDP-N-acetylglucosamine 4-epimerase increases during spherulation, microplasmodium
Manually annotated by BRENDA team
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specific activity of the enzyme increases at the later stage of sporulation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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determined by SDS-PAGE and MALDI-TOF mass spectrometry
37800
predicted by amino acid sequence
62000
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gel filtration
80000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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sequence comparisons and structure homology modeling, overview. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant H305A enzyme, best by microbatch under oil set up and hanging drop vapor diffusion method, from a solution containing 25% PEG 3350, 0.2 M ammonium sulfate, cryoprotection by 15-20% glycerol, X-ray diffraction structure determination and analysis at 2.10 A resolution
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microbatch under oil method, using 250 mM ammonium sulfate, 100 mM Bis-Tris pH 6.5, (25% w/v) PEG 3350
hanging drop vapor diffusion method, crystal structure of the enzyme in complex with cofactor and either UDP-glucose or UDP-N-acetyl-D-galactosamine, determined at 2.5 and 2.1 A, crystals belong to the space group P222(1), with unit cell dimensions of a = 61 A, b = 96 A, and c = 140 A
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
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4°C, stable
2411
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
half-life is 13.5 h
50
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pH 7.5, 15 min, 65% loss of activity in presence of 1 mM NAD+, in absence of NAD+ complete loss of activity
60
-
half-life is 23 min
80
-
treatment at 80 °C for 30 min reduces the enzyme activity by 78%
90
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enzyme is stable at 90°C; after incubating at this temperature for 10 min, 90% of the enzymatic activity remains
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes the enzyme increasing its lifetime in the reaction mixture by 50%
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration
by using nickel-NTA affinity chromatography
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MalE-Gne fusion protein
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nickel-Sepharose column chromatography
recombinant enzyme
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recombinant N-termminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein
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gene galE, expression of N-termminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene gne, phylogenetic analysis
gene gne2, phylogenetic analysis; gene gne, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production
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spores produced by a mutant strain lacking the enzyme still contain normal levels of BclA-attached oligosaccharides, monosaccharide analysis of the oligosaccharides reveals that N-acetylglucosamine had replaced N-acetylgalactosamine, significant levels of gene transcripts are detected only during sporulation, an observation consistent with a role for this gene in exosporium assembly, gene expression during sporulation appears to be biphasic
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H305A
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site-directed mutagenesis, structure determination and analysis, the mutant shows reduced activity with UDP-N-acetylglucosamine
S144T/H305A
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A/S306Y
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site-directed mutagenesis, the mutant shows no activity with either UDP-GlcNAc or UDP-Glc
G118A/G119A
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
G188S/G119S
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S116A
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S279Y
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
T117S
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site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
A209N
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mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and very limited epimerization activity with UDP-D-glucose and UDP-D-galactose
G102K
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mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and no epimerization activity with UDP-D-glucose and UDP-D-galactose
Q201E
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mutant enzyme shows slightly epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type activity and very limited epimerization activity with UDP-D-Glc and UDP-D-Gal
Q201E/G102K
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mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine, no epimerization activity with UDP-D-glucose and very limited activity with UDP-D-galactose
S143A
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mutant enzyme shows epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type enzyme and no epimerization activity with UDP-D-glucose and UDP-D-galactose
S144K
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mutant enzyme shows no epimerization activity with UDP-N-acetyl-D-glucosamine/UDP-N-acetyl-D-galactosamine and UDP-D-glucose/UDP-D-galactose
S306Y
-
completely inactive mutant enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
mutant deficient for gne shows increased surface hydrophobicity, produces deep alterations in the outer membrane architecture, and displays noticeable increases in the sensitivity to microcidal peptides, to eel and human sera, and to phagocytosis/opsonophagocytosis. Significant attenuation of virulence for eels and mice is observed with the mutant, which is correlated with the loss of the O-antigen lipopolysaccharide, while the capsule is maintained
synthesis
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