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Information on EC 5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase
for references in articles please use BRENDA:EC5.1.3.7
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EC Tree 5 Isomerases
5.1 Racemases and epimerases
5.1.3 Acting on carbohydrates and derivatives
5.1.3.7 UDP-N-acetylglucosamine 4-epimerase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 5.1.3.7
-
emirates
- artery
- albumin
- urinary
- uterine
-
embolization
- women
-
microalbuminuria
- fibroid
-
ultrasound
- hypertension
-
ultrasound-assisted
-
symptomatic
- mellitus
- cardiovascular
- nephropathy
-
glomerular
- pregnancy
-
hysterectomy
- creatinine
- albuminuria
-
systolic
- bleeding
-
gulf
-
diastolic
-
ultrasonic
-
dubai
-
ambulatory
- arabia
-
cesarean
-
normoalbuminuric
-
myomectomy
-
antihypertensive
-
microwave-assisted
- menorrhagia
-
curettage
-
qatar
- myoma
- adenomyosis
-
box-behnken
-
hypertensives
-
kuwait
-
leiomyomata
-
postprocedural
-
citizens
-
soxhlet
-
satisfaction
-
radiologist
- synthesis
- medicine
-
transvaginal
-
preprocedural
showSynonyms
uae, udp-n-acetylglucosamine 4-epimerase, udp-n-acetylglucosamine 4'-epimerase, udp-galnac 4-epimerase, udp-glcnac epimerase, gne epimerase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Epimerase, uridine diphosphoacetylglucosamine
-
-
-
-
GalE
GNE
Gne epimerase
group 3 epimerase
KfoA
UDP acetylglucosamine epimerase
-
-
-
-
UDP-GalNAc 4-epimerase
UDP-GlcNAc epimerase
UDP-hexose 4-epimerase
UDP-N-acetylglucosamine 4'-epimerase
member of the short-chain dehydrogenase/reductase superfamily
UDP-sugar 4-epimerase
Uridine 5'-diphospho-N-acetylglucosamine-4-epimerase
-
-
-
-
Uridine diphosphate N-acetylglucosamine-4-epimerase
-
-
-
-
Uridine diphosphoacetylglucosamine epimerase
-
-
-
-
WbgU
WbPP
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
reaction mechanism of KfoA
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
reaction mechanism of KfoA
Escherichia coli ATCC 23502 / K4
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
epimerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
teichuronic acid biosynthesis (B. subtilis 168), UDP-N-acetyl-D-galactosamine biosynthesis I, 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
9024-16-2
-
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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-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
Substrates: epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
Substrates: -
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
-
Substrates: the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
-
Substrates: the achieved reasonable conversion rates the amount of enzyme used is increased 200fold comparted to UDP-N-acetyl-D-glucosamine as substrate. Substrate conversions reach 20% for UDP-Glc and 65% for UDP-Gal
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
-
Substrates: unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-Glc and UDP-Gal than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Escherichia coli ATCC 23502 / K4
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: r
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: r
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: r
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: equilibrium reaction resulting in a 70:30 ratio of UDP-GlcNAc to UDP-GalNAc, irrespective of the initial substrate
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: wild-type enzyme is more efficient in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine than in catalyzing the epimerization of UDP-glucose and UDP-galactose
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
Q81JK4
Substrates: -
Products: -
Products: -
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
Substrates: GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
Products: -
Products: -
r
additional information
?
-
Q81JK4
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of KfoA, overview. KfoA epimerizes both acetylated and non-acetylated (UDP-Glc) substrates, EC 5.1.3.2, but its kcat/Km value for UDP-GlcNAc is approximately 1300fold that for UDP-Glc. Recombinant KfoA showes a strong preference for acetylated substrates in vitro. Coupling of K4 chondroitin polymerase (KfoC) and KfoA to determine the activity of UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
Escherichia coli ATCC 23502 / K4
Substrates: substrate specificity of KfoA, overview. KfoA epimerizes both acetylated and non-acetylated (UDP-Glc) substrates, EC 5.1.3.2, but its kcat/Km value for UDP-GlcNAc is approximately 1300fold that for UDP-Glc. Recombinant KfoA showes a strong preference for acetylated substrates in vitro. Coupling of K4 chondroitin polymerase (KfoC) and KfoA to determine the activity of UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
Products: -
Products: -
?
additional information
?
-
Substrates: the group 3 epimerase WbpP from Pseudomonas aeruginosa is very specific for N-acetylated substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulates gastric mucous aminosugar metabolism
Products: -
Products: -
?
additional information
?
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TMGalE also has high activity for epimerization of UDP-Gal to UDP-Glc, EC 5.1.3.2. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms
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-D-glucose
UDP-D-galactose
-
Substrates: the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
Products: -
Products: -
r
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Escherichia coli ATCC 23502 / K4
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
Substrates: the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20
Products: -
Products: -
?
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
Q81JK4
Substrates: -
Products: -
Products: -
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
Substrates: GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
Products: -
Products: -
r
additional information
?
-
Q81JK4
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulates gastric mucous aminosugar metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
enzyme-bound, exogenous NAD+ does not appear to be a strong activator of enzyme activity, there is no significant difference in enzyme activity regardless of the presence and absence of NAD+
NAD+
the N-terminal domain harbors the conserved sequence GxxGxxG forming a modified Rossmann-fold involved in binding of the cofactor NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-{(E)-[(6-bromo-2-hydroxynaphthalen-1-yl)methylidene]amino}-5'-deoxyuridine
-
IC50: 0.025 mM, specific for UDP-GlcNAc 4-epimerase, powerful reagent for reversible inhibition of O-linked glycosylation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-[2-(Diethylamino)ethyl]amino-5,11-dihydro[1]benzoxepino[3,4-b]pyridine trihydrochloride
-
stimulates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
2.4
UDP-N-acetyl-alpha-D-galactosamine
recombinant enzyme, pH 7.0, 80°C