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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase
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5.1.3.2 UDP-glucose 4-epimeraseIUBMB Comments
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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Word Map
- 5.1.3.2
- polysaccharide
- galactokinase
-
leloir
- galactosemia
- galactose-1-phosphate
- udp-galnac
- udp-n-acetylglucosamine
-
galactose-inducible
-
uridylyltransferase
- fragilis
-
kluyveromyces
-
pyrophosphorylase
- udp-n-acetylgalactosamine
- udp-sugars
- udpglucose
- galnac
- mutarotase
-
galactose-containing
-
udp-glucuronic
-
o-antigens
- medicine
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
4-Epimerase, 6xHis-rGalE, ABD1_580, An14g03820, AtUGE1, AtUGE2, AtUGE3, AtUGE4, AtUGE5, CaGAL10, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-Epimerase
-
-
-
-
ABD1_580
An14g03820
epimerase Ab-WbjB
Epimerase, uridine diphosphoglucose
-
-
-
-
fnlA
GAL10
Gal10p
Galactowaldenase
GalE
galE-1
galE1
GalESp1
GalESp2
GNE
H3634
HvUGE1
HvUGE2
Rv3634c
TM0509
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-Gal 4-epimerase
UDP-Gal/Glc 4-epimerase
UDP-galactose 4'-epimerase
UDP-galactose 4-epimerase
UDP-galactose-4'-epimerase
UDP-galactose-4-epimerase
UDP-Glc 4-epimerase
UDP-GlcNAc/Glc 4-epimerase
UDP-glucose 4-epimerase
UDP-glucose 4-epimerase 4
UDP-glucose epimerase
-
-
-
-
UDP-glucose-4-epimerase
UDP-glucose/-galactose 4-epimerase
UDP-hexose 4-epimerase
UDP-N-acetyl-glucosamine 4,6-dehydratase
UDP-sugar 4-epimerase
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
UGE
UGE1
Uge1p
UGE2
UGE3
UGE4
UGE5
UgeA
Uridine diphosphate galactose 4-epimerase
Uridine diphosphate glucose 4-epimerase
-
-
-
-
uridine diphosphate-galactose-4'-epimerase
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
WbjB
additional information
Gal10p
-
the first and the last enzyme of the Leloir pathway, galactose mutarotase and UDP-galactose 4-epimerase, are comtained within a single polypeptide chain referred to as Gal10p
Galactowaldenase
-
-
-
-
UDP-galactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
-
additional information
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
cf. EC 5.1.3.7
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
-
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
presence of at least one essential Arg at the substrate-binding region of the active site
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
Ser124 and Tyr149 are likely to play important roles in the catalytic mechanism
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
a nucleoside diphospho-4-ulose of the configuration D-xylo-4-hexosulose is an intermediate in the reaction
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
structurereactivity studies and reaction mode, acid-base catalysis of hydride transfer, overview
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
revolving door reaction mechanism, Tyr149 is the base catalyst for hydride transfer, overview. The enzyme undergoes a conformational change upon binding of the UDP sugar, which is in fact a result of the binding of the UMP-moiety of the substrate. The conserved lysine from the YxxxK motif plays an important role in the activation of the cofactor, as due to the conformational change, the 6-ammonium group is hydrogen-bonded to both the 2'- and 3'-hydroxylgroups of the nicotinamide riboside of NAD+
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
additional information
epimerization
-
-
specificity for carbon 4, forming a 4-hexosulose intermediate
-
epimerization
-
of uridine diphosphate (UDP)-glucose to a galactose derivated UDP-galactose
epimerization
-
The reaction mechanism of UGE is thought to occur via transfer of the 4'-OH hydrogen of the sugar to the nicotinamide ring of noncovalently bound NAD+, rotation of the resulting 4'-ketopyranose intermediate in the active site, and transfer of the hydride from the nicotinamide ring of NADH back to C-4 of the sugar.
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
-
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
-
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
colanic acid building blocks biosynthesis, D-galactose degradation I (Leloir pathway), D-galactose detoxification, mycolyl-arabinogalactan-peptidoglycan complex biosynthesis, stachyose degradation, superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis, UDP-alpha-D-galactose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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CAS REGISTRY NUMBER
COMMENTARY
9032-89-7
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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
D-galactose
D-glucose
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-tagatose
D-fructose
the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
-
-
?
UDP-L-arabinose
UDP-D-xylose
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
-
-
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
the NAD+-dependent enzyme is responsible for reversibly inverting the 4-hydroxyl configuration of UDP-alpha-D-galactose to form UDP-alpha-D-glucose
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
via 4-ketose intermediate
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
via 4-ketose intermediate, UDP-glucose is bound within the active site cleft, substrate binding structure, overview
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
with NAD+ as cofactor, UDP-4-ketopyranose and NADH are reaction intermediates. Weak binding of the 4-ketopyranosyl moiety and strong binding of the UDP-moiety within a substrate domain allow either face of the 4-ketopyranosyl moiety to accept hydride from NADH, pH-dependent charge transfer complex between Tyr149 and NAD+
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
reaction mechanism modelling, overview
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-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
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-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
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-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
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-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
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the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
residues Ser123, Tyr147, Asn177, Asn197, Arg229, Arg290, Asp293,and Tyr297 play a role in UDP-sugar binding
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
residues Ser123, Tyr147, Asn177, Asn197, Arg229, Arg290, Asp293,and Tyr297 play a role in UDP-sugar binding
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
r
UDP-D-xylose
UDP-L-arabinose
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-galactose
UDP-glucose
-
RDH1 is a likely target of root-specific negative regulation by ethylene and loss of RDH1 function results in a heightened sensitivity of root tissues to both ethylene and auxin
-
-
?
UDP-galactose
UDP-glucose
-
the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide
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-
r
UDP-galactose
UDP-glucose
-
role of the essential arginine residue in stretching and binding of the substrate
-
?
UDP-galactose
UDP-glucose
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enzyme catalyzes the first step of the Lelpoir pathway
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-
r
UDP-galactose
UDP-glucose
-
enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
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r
UDP-galactose
UDP-glucose
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point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
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r
UDP-galactose
UDP-glucose
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UDP-galacturonic acid C4-epimerase also interconverts UDP-galactose and UDP-glucose, albeit at much lower activity than the interconversion of UDP-galacturonate and UDP-glucuronic acid
-
-
r
UDP-galactose
UDP-glucose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
-
-
r
UDP-galactose
UDP-glucose
-
Leloir pathway of D-galactose catabolism
-
-
?
UDP-galactose
UDP-glucose
-
Leloir pathway of galactose metabolism
-
-
r
UDP-galactose
UDP-glucose
glycolysis and TCA cycle, Leloir pathway
-
-
r
UDP-GalNAc
UDP-GlcNAc
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the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide. The enzyme supplies the UDP-GalNAc required for the synthesis of the capsule
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-
r
UDP-GalNAc
UDP-GlcNAc
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enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
-
-
r
UDP-GlcNAc
UDP-GalNAc
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wild-type enzyme shows no interconversion of UDP-GlcNAc and UDP-GalNAc, mutation Y299C results in a gain of activity against UDP-GalNAc by more than 230fold
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
-
-
r
additional information
?
-
-
Leloir pathway of galactose metabolism
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?
additional information
?
-
Q81JK4
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
-
-
?
additional information
?
-
Q81K34
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
-
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?
additional information
?
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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
-
-
?
additional information
?
-
Q81JK4
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
-
Q81K34
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
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UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
-
Q81JK4
no activity with UDP-N-acetylgalactoseamine
-
-
?
additional information
?
-
Q81K34
no activity with UDP-N-acetylgalactoseamine
-
-
?
additional information
?
-
-
no activity with UDP-N-acetylgalactoseamine
-
-
?
additional information
?
-
-
TDP-[4-3H]glucose donates tritium to enzyme-bound NAD+, leading to formation of enzyme-[3H1]NADH. This suggests that a nucleoside diphospho-4-ulose of the configuration D-xylo-4-hexosulose is an intermediate in the reaction
-
-
?
additional information
?
-
-
no interconversion of UDP-GalNAc and UDP-GlcNAc
-
-
?
additional information
?
-
no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
-
-
?
additional information
?
-
-
no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
-
-
?
additional information
?
-
Escherichia coli GalE is unable to catalyse the epimerization of acetylated substrates due to the so-called gatekeeper wall of the active site substrate-binding hexagonal box that is occupied by a bulky residue, Tyr299
-
-
?
additional information
?
-
-
catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism
-
?
additional information
?
-
-
impairement of the enzyme results in galacosemia III that can lead to symptoms ranging from benign to severe
-
?
additional information
?
-
-
the epimerase shows associated mutarotase activity distinct from the constitutively formed mutarotase activity. Both activities exist in two functionally independent domains
-
?
additional information
?
-
-
the enzyme plays an essential role in exopolysaccharide formation. Exopolysaccharide synthesis is considerably improved at a controlled pH of 5.0 on galactose as carbon source, and is correlated with higher-induced activities of UDP-glucose pyrophosphorylase and UDP-galactose 4-epimerase under these growth conditions
-
?
additional information
?
-
Lacticaseibacillus casei CL 87
-
the enzyme plays an essential role in exopolysaccharide formation. Exopolysaccharide synthesis is considerably improved at a controlled pH of 5.0 on galactose as carbon source, and is correlated with higher-induced activities of UDP-glucose pyrophosphorylase and UDP-galactose 4-epimerase under these growth conditions
-
?
additional information
?
-
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
-
-
?
additional information
?
-
-
the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2
-
-
?
additional information
?
-
the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
-
-
?
additional information
?
-
the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
-
-
?
additional information
?
-
-
the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
-
-
?
additional information
?
-
the bifunctional UDP-Glc 4-epimerase/UDP-Xyl 4-epimerase in the cytosol is distinct from the UDP-Xyl 4-epimerase in the Golgi apparatus, the two activities of UGE1 occur at the same catalytic site. No activity with UDP-N-acetylglucosamine or UDP-glucuronic acid, UGE1 substrate specificity, overview
-
-
?
additional information
?
-
-
the bifunctional UDP-Glc 4-epimerase/UDP-Xyl 4-epimerase in the cytosol is distinct from the UDP-Xyl 4-epimerase in the Golgi apparatus, the two activities of UGE1 occur at the same catalytic site. No activity with UDP-N-acetylglucosamine or UDP-glucuronic acid, UGE1 substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
-
-
?
additional information
?
-
-
UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The epimerase and mutarotase activities are located in different regions of the epimerase holoenzyme
-
?
additional information
?
-
the bifunctional enzyme GAL10 also exhibits galactose mutarotase activity, EC 5.1.3.3
-
-
?
additional information
?
-
Saccharomyces cerevisiae ATCC 204508 / S288c
the bifunctional enzyme GAL10 also exhibits galactose mutarotase activity, EC 5.1.3.3
-
-
?
additional information
?
-
Saccharomyces fragilis
-
enzyme may play a regulatory role in controlling the flux of galactose metabolism
-
-
?
additional information
?
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
Uge1 protein contains only one epimerase domain
-
-
?
additional information
?
-
-
Uge1 protein contains only one epimerase domain
-
-
?
additional information
?
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
Uge1 protein contains only one epimerase domain
-
-
?
additional information
?
-
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, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
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, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
-
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, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
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, 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. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
-
-
?
additional information
?
-
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, 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. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
-
-
?
additional information
?
-
-
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, 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. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
-
-
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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, 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. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
-
-
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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, 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. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
-
-
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
-
enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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
-
-
?
additional information
?
-
-
both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms
-
-
?
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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-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
the NAD+-dependent enzyme is responsible for reversibly inverting the 4-hydroxyl configuration of UDP-alpha-D-galactose to form UDP-alpha-D-glucose
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
via 4-ketose intermediate
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
r
UDP-galactose
UDP-glucose
-
the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide
-
-
r
UDP-galactose
UDP-glucose
-
enzyme catalyzes the first step of the Lelpoir pathway
-
-
r
UDP-galactose
UDP-glucose
-
enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
-
-
r
UDP-galactose
UDP-glucose
-
point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
-
-
r
UDP-galactose
UDP-glucose
-
Leloir pathway of D-galactose catabolism
-
-
?
UDP-galactose
UDP-glucose
-
Leloir pathway of galactose metabolism
-
-
r
UDP-galactose
UDP-glucose
glycolysis and TCA cycle, Leloir pathway
-
-
r
UDP-GalNAc
UDP-GlcNAc
-
the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide. The enzyme supplies the UDP-GalNAc required for the synthesis of the capsule
-
-
r
UDP-GalNAc
UDP-GlcNAc
-
enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
-
-
r
additional information
?
-
-
Leloir pathway of galactose metabolism
-
-
?
additional information
?
-
Q81JK4
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
-
-
?
additional information
?
-
Q81K34
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Q81JK4
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
-
Q81K34
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
-
-
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
?
additional information
?
-
-
impairement of the enzyme results in galacosemia III that can lead to symptoms ranging from benign to severe
-
?
additional information
?
-
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
-
-
?
additional information
?
-
Saccharomyces fragilis
-
enzyme may play a regulatory role in controlling the flux of galactose metabolism
-
-
?
additional information
?
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
?
additional information
?
-
-
both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
NAD+
Torulopsis candida
-
depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+
NAD+
-
absolute requirement for NAD+. Km: 0.27 mM for the liver enzyme, Km: 0.28 mM for the mammary enzyme
NAD+
-
two nicotinamide cofactors bind in symmetry-related positions in the dimer
NAD+
-
NAD+ is very tightly but noncovalently bound in the active site, NAD+ is reduced to NADH in the course of catalysis. NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth
NAD+
coenzyme is tightly bound at the active site. NAD+ functions as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating their dehydrogenation to the common intermediate UDP-4-ketohexopyranoside. NAD+ activation induced by uridine nucleotides is brought about by a conformational change of epimerase that repositions Tyr149 at an increased distance from nicotinamide N1 of NAD+ while maintaining the electrostatic repulsion between Lys153 and nicotinamide N1 of NAD+
NAD+
-
the amino acid side chains responsible for anchoring the NAD+ to the protein include Asp33, Asn37, Asp66, Tyr157 and Lys161
NAD+
-
1.78 mol of NAD+ per dimer. Each subunit is independently capable of being associated with one molecule of NAD+, suggestive of two NAD+ binding sites of epimerase per dimer
NAD+
bound within the active site cleft, binding structure, overview
NAD+
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
NAD+
-
the fully active GalE is dimeric and contains one tightly bound NAD+ per subunit, NAD+ undergoes reversible reduction to NADH in the chemical mechanism, practically irreversible binding of NAD+ within a Rossmann-type fold, nonstereospecific hydride transfer, uridine nucleotide-induced activation of NAD, Tyr149 as a base catalyst, and [GalE-NADH]-oxidation in one-electron steps by one-electron acceptors. pH-Dependent charge transfer complex between Tyr149 and NAD+. Binding structure, overview
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+
NAD+
the NAD+ cofactor can be removed from human GalE without denaturation. Fewer protein-NAD+ contacts are observed in the crystal structure, which explains the reversible character of cofactor binding
NAD+
two paired Rossmann folds tightly bind one NAD+ cofactor per subunit. In Escherichia coli GalE, the NAD+ interacts more extensively with the protein than is observed with other SDR enzymes. pH-Dependent charge transfer complex between Tyr149 and NAD+
additional information
an NAD+ binding motif is GGXGXXG, not required for activity
-
additional information
-
an NAD+ binding motif is GGXGXXG, not required for activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
Ba2+
enzyme activity is 54.6 U/mg protein at a metal concentration of 1 mM
Ca2+
enzyme activity is 47.8 U/mg protein at a metal concentration of 1 mM
Co2+
enzyme activity is 44.7 U/mg protein at a metal concentration of 1 mM
Cu2+
enzyme activity is 21.8 U/mg protein at a metal concentration of 1 mM
Fe3+
enzyme activity is 20.3 U/mg protein at a metal concentration of 1 mM
Li+
enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
Mg2+
Mn2+
Zn2+
enzyme activity is 17.2 U/mg protein at a metal concentration of 1 mM
additional information
Mg2+
enzyme activity is 51.5 U/mg protein at a metal concentration of 1 mM
Mn2+
enzyme activity is 43.2 U/mg protein at a metal concentration of 1 mM
additional information
no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
additional information
-
no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
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+
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
1,2-Cyclohexanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2',3'-O-(2,4,6-Trinitrocyclohexadienylidene)uridine 5'-monophosphate
-
powerful reversible inhibitor
2-Hydroxy-5-nitrobenzyl bromide
-
a combination of NAD+ and UDP protects against modification
5,5'-dithiobis(2-nitrobenzoate)
Saccharomyces fragilis
-
reactivation in presence of mercaptoethanol, protection by UDPglucose or UDPgalactose, inactivated enzyme retains the dimeric structure and NAD+ is not dissociated from the protein moiety
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
fructose 1,6-diphosphate
-
inhibition is enhanced by combination with UMP
Galactose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
L-Xylose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
PCMB
-
dissociates the native epimerase into inactive mercurated monomers, reconstitution of the functional holoenzyme is done by reduction with dithiothreitol and addition of extra NAD+, reactivation is most effective at pH 8.1
Sodium cyanoborohydride
-
NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction, mutant proteins K153M and K153A bind UMP very well, but the rate at which NAD+ associated with them is reduced by sodium cyanoborohydride is almost insensitive to the presence of UMP
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
5'-UMP
-
the native enzyme is completely insensitive to inhibition, the desensitized enzyme is strongly inhibited. Desensitization by heat converts the enzyme to its ultimate catalytic form
5'-UMP
-
string competitive inhibitor. The enzyme contains 0.77 mol of 5'-UMP per dimer
5'-UMP
-
a competitive, irreversible inhibitor, binds per dimer of epimerase as isolate and causes inactivation, transition profiles indicate the existence of a stable intermediate with one inhibitor-binding site remaining unoccupied. Reductive inhibition of this intermediate reduces the activity to 58% with modification of one catalytic site, negative cooperativity, inhibition mechanism, overview. Protective effect of 5'-UMP against modification of the arginine located at the catalytic site by 1,2-cyclohexanedione
5'-UMP
-
epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
-
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
-
-
diethyldicarbonate
-
almost complete inhibition at 5 mM after 30 min incubation
diethyldicarbonate
-
reversal of inhibition by hydroxylamine. Modification of 1 essential histidine residue is responsible for loss in catalytic activity
galactose 6-phosphate
-
activation of the minor enzyme form; partial inhibition of major enzyme form
glucose 1-phosphate
-
partial inhibition of minor enzyme form, no effect on major enzyme form
glucose 1-phosphate
-
partial inhibition of minor enzyme form, no effect on major enzyme form
glucose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
-
glucose plus UMP
-
NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction by sugars such as glucose and arabinose, but the mutant proteins K153M and K153A are not reduced by sugars in the presence or absence of UMP
-
L-arabinose
-
on treatment with L-arabinose, 2 mM, in presence of UMP, 0.5 mM, both the native enzyme and the reconstituted enzyme are inactivated at an indistinguishable rate of inactivation
L-arabinose
-
epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-Arabinose plus UMP or UDP
-
NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction by sugars such as glucose and arabinose, but the mutant proteins K153M and K153A are not reduced by sugars in the presence or absence of UMP
-
L-Arabinose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
NADH
-
NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth
p-chloromercuribenzoate
-
no inactivation by p-chloromercuribenzoate
additional information
-
inhibited by combination of 100 microM NADH and 10 microM NAD+
-
additional information
-
no inactivation by the UDP-D-fucose or D-fucose alone or by UDP-D-fucose plus 5'-UMP
-
additional information
-
NAD+ associated with the wild type enzyme is also subject to UMP-dependent reduction by sodium cyanoborohydride. The mutant protein binds UMP very well, but the rate at which NAD+ associated with them is reduced by sodium cyanoborohydride is almost insensitive to the presence of UMP. The purified wild type enzyme contains significant amounts of NADH bound to the coenzyme site, however the purified mutants K153M and K153A contain very little NADH
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
non-covalently bound, released from the enzyme after denaturation with aqueous ethanol. Each enzyme molecule contains one molecule of NAD+
additional information
-
does not require external NAD+ for activity
-
Galactose 1-phosphate
-
activation of minor enzyme form, no effect on major enzyme form
Galactose 1-phosphate
-
activation of minor enzyme form, no effect on major enzyme form
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Cataract
[Early childhood cataract in hereditary UDP-galactose-4-epimerase deficiency--a case report]
Cysts
Mutation of a UDP-glucose-4-epimerase alters nematode susceptibility and ethylene responses in Arabidopsis roots.
Fanconi Syndrome
Defective galactose oxidation in a patient with glycogen storage disease and Fanconi syndrome.
galactokinase deficiency
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
Galactosemias
A Case Study of Monozygotic Twins Apparently Homozygous for a Novel Variant of UDP-Galactose 4'-epimerase (GALE) : A Complex Case of Variant GALE.
Galactosemias
A new mass screening method of detecting UDP-galactose-4-epimerase deficiency.
Galactosemias
A specific enzymatic assay for the diagnosis of congenital galactosemia. II. The combined test with 4-epimerase.
Galactosemias
Altered cofactor binding affects stability and activity of human UDP-galactose 4'-epimerase: Implications for type III galactosemia.
Galactosemias
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
Galactosemias
Characterization of two mutations associated with epimerase-deficiency galactosemia, by use of a yeast expression system for human UDP-galactose-4-epimerase.
Galactosemias
Coordinated movement, neuromuscular synaptogenesis and trans-synaptic signaling defects in Drosophila galactosemia models.
Galactosemias
Detection of UDP-galactose-4-epimerase deficiency in a galactosemia screening program.
Galactosemias
Developmental defects in a Caenorhabditis elegans model for type III galactosemia.
Galactosemias
Functional analysis of mutations in UDP-galactose-4-epimerase (GALE) associated with galactosemia in Korean patients using mammalian GALE-null cells.
Galactosemias
Functional characterization of the K257R and G319E-hGALE alleles found in patients with ostensibly peripheral epimerase deficiency galactosemia.
Galactosemias
Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia.
Galactosemias
In silico prediction of the effects of mutations in the human UDP-galactose 4'-epimerase gene: towards a predictive framework for type III galactosemia.
Galactosemias
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
Galactosemias
Liquid Chromatography-Tandem Mass Spectrometry Enzyme Assay for UDP-Galactose 4'-Epimerase: Use of Fragment Intensity Ratio in Differentiation of Structural Isomers.
Galactosemias
Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
Galactosemias
Molecular dynamics, residue network analysis, and cross-correlation matrix to characterize the deleterious missense mutations in GALE causing galactosemia III.
Galactosemias
The metastability of human UDP-galactose 4'-epimerase (GALE) is increased by variants associated with type III galactosemia but decreased by substrate and cofactor binding.
Galactosemias
The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients.
Galactosemias
[Effectiveness of the screening programme for galactosemia. New strategy in Poland]
Genetic Diseases, Inborn
Analysis of UDP-galactose 4'-epimerase mutations associated with the intermediate form of type III galactosaemia.
Genetic Diseases, Inborn
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
Infections
Brucella melitensis 16M: characterisation of the galE gene and mouse immunisation studies with a galE deficient mutant.
Infections
Developmental defects in a Caenorhabditis elegans model for type III galactosemia.
Infections
Schistosoma Japonicum UDP-Glucose 4-Epimerase Protein Is Located on the Tegument and Induces Moderate Protection against Challenge Infection.
Liver Failure
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Muscle Hypotonia
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Neoplasms
Carbon Source Affects Synthesis, Structures, and Activities of Mycelial Polysaccharides from Medicinal Fungus Inonotus obliquus.
Neoplasms
DNA sequence-dependent variation in nucleosome structure, stability, and dynamics detected by a FRET-based analysis.
Neoplasms
Metabolic inhibition of mammalian uridine diphosphate galactose 4-epimerase in cell cultures and in tumor cells.
Neoplasms
Sequence-dependent nucleosome structure and stability variations detected by Förster resonance energy transfer.
Osteoarthritis
The critical role of UDP-galactose-4-epimerase in osteoarthritis: modulating proteoglycans synthesis of the articular chondrocytes.
Starvation
Functional complementation of a membrane transport deficiency in Saccharomyces cerevisiae by recombinant ND4 fusion protein.
Starvation
Galactose starvation in a bloodstream form Trypanosoma brucei UDP-glucose 4'-epimerase conditional null mutant.
Stomach Neoplasms
Overexpression of UDP-Glucose 4-Epimerase Is Associated with Differentiation Grade of Gastric Cancer.
Thrombocytopenia
Inherited thrombocytopenia associated with mutation of UDP-galactose-4-epimerase (GALE).
Thrombocytopenia
Myelodysplasia and deficiency of uridine diphosphate-galactose 4-epimerase.
Trypanosomiasis, African
The molecular dynamics of Trypanosoma brucei UDP-galactose 4'-epimerase: a drug target for African sleeping sickness.
Tuberculosis
Rv3634c from Mycobacterium tuberculosis H37Rv encodes an enzyme with UDP-Gal/Glc and UDP-GalNAc 4-epimerase activities.
udp-glucose 4-epimerase deficiency
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
udp-glucose 4-epimerase deficiency
A first case report of UDP-galactose-4'-epimerase deficiency in China: genotype and phenotype.
udp-glucose 4-epimerase deficiency
A new mass screening method of detecting UDP-galactose-4-epimerase deficiency.
udp-glucose 4-epimerase deficiency
A new method of screening for inherited disorders of galactose metabolism.
udp-glucose 4-epimerase deficiency
Detection of UDP-galactose-4-epimerase deficiency in a galactosemia screening program.
udp-glucose 4-epimerase deficiency
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
udp-glucose 4-epimerase deficiency
Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
udp-glucose 4-epimerase deficiency
Myelodysplasia and deficiency of uridine diphosphate-galactose 4-epimerase.
udp-glucose 4-epimerase deficiency
Reversal of UDP-galactose 4-epimerase deficiency of human leukocytes in culture.
udp-glucose 4-epimerase deficiency
Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4'-epimerase deficiency. IV. Report of eight cases in three families.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4-epimerase deficiency.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4-epimerase deficiency. II. Clinical follow-up, biochemical studies and family investigation.
Vaccinia
Expansion of the mammalian 3 beta-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
UDP-D-glucose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
2 - 6
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
83
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
110
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
230
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
260
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
0.057
UDP-D-galactose
recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.068
UDP-D-galactose
recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.087
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.095
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDPGlc dehydrogenase
0.15
UDP-D-galactose
recombinant enzyme UGE5, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
0.29
UDP-D-galactose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.048
UDP-galactose
-
wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C
0.1 - 0.13
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.17 - 0.22
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.19 - 0.22
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.2
UDP-galactose
-
mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C
0.23 - 0.3
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.25
UDP-galactose
-
mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C
0.258
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
0.38
UDP-galactose
-
wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C
0.5
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
0.8
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
1
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
0.09
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.13
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.19
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.56
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.76
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.146
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
0.243
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
0.316
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
0.362
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
0.426
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
0.437
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
0.14
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
additional information
additional information
Saccharomyces fragilis
-
classical hyperbolic kinetics with UDPgalactose, allosteric kinetics with UDPglucose
-
additional information
additional information
Saccharomyces fragilis
-
enzyme shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
biphasic Michaelis-Menten kinetics, kinetic patterns, overview. Michaelis-Menten relationship of the monomeric epimerase shows hyperbolic dependency
-
additional information
additional information
kinetic analyis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic analyis of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.073
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
0.61
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
0.67
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
250
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
760
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
9
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme
20
UDP-D-galactose
recombinant enzyme UGE4
27
UDP-D-galactose
recombinant enzyme UGE3
55
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE2
64
UDP-D-galactose
recombinant enzyme UGE5
0.633
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
23 - 24
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
28 - 34
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
42 - 66
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
46
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
89 - 101
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
115 - 128
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
116
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
199.1
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
2 - 8
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5â9 mM).
19
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5â9 mM).