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Enzyme Nomenclature
Information on EC 5.1.3.2 - UDP-glucose 4-epimerase
for references in articles please use BRENDA:EC5.1.3.2
Word Map on EC 5.1.3.2
- 5.1.3.2
- galactokinase
-
leloir
- galactosemia
- galactose-1-phosphate
- fragilis
-
galactose-inducible
-
kluyveromyces
- udp-n-acetylglucosamine
- udp-galnac
-
pyrophosphorylase
-
uridylyltransferase
- udp-n-acetylgalactosamine
- udp-sugars
- udpglucose
-
exopolysaccharide
- mutarotase
- galnac
-
o-antigens
-
galactose-containing
- medicine
- synthesis
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
5.1.3.2
-
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RECOMMENDED NAME
GeneOntology No.
UDP-glucose 4-epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
; presence of at least one essential Arg at the substrate-binding region of the active site; 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
structurereactivity studies and reaction mode, acid-base catalysis of hydride transfer, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
additional information
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.
epimerization
-
-
specificity for carbon 4, forming a 4-hexosulose intermediate
-
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc; HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
catalyses the interconversion of UDP-Gal and UDPGlc; HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc; 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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure
evolution
-
the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
evolution
-
the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
-
malfunction
-
GALE deficiency leads to mild or severe disease with clinical symptoms similar to classical galactosemia
malfunction
-
UDP-galactose-4-epimerase deficiency causes galactosemia. Altered protein stability is due to misfolding and loss or reduction of enzyme activity is responsible for the molecular defects underlying GALE-deficiency galactosemia
malfunction
-
In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
malfunction
-
In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
-
metabolism
-
GALE catalyzes the third step of the Leloir pathway of galactose metabolism
metabolism
-
UgeA interconverts UDP-glucose and UDP-galactose and participates in galactose metabolism
metabolism
-
overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
metabolism
-
the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
metabolism
-
overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
-
metabolism
-
the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
-
physiological function
-
galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
-
enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis, gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis; galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
-
GalE plays a key role in lipopolysaccharide biosynthesis
physiological function
-
UDP-Gal provides all galactosyl units in biologically synthesized carbohydrates. All healthy cells produce UDP-Gal from uridine 5'-diphospho-alpha-D-glucose UDP-Glc, by the action of UDP-galactose 4-epimerase
physiological function
-
Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
physiological function
the enzyme induces moderate protection against challenge infection
physiological function
-
the enzyme produces the precursor UDP-galactopyranose required for galactofuranose synthesis
physiological function
-
Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
-
additional information
-
ligand-bound enzyme structures, active site structure including Lys153, Tyr149, and Ser124, overview
additional information
-
structure homology modeling, overview. The Marinithermus enzyme makes use of a TxnYx3K catalytic triad rather than the usual SxnYx3K triad. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine, the gatekeeper residue is responsible for the substrate specificity, the two consecutive glycine residues, Gly118 and Gly119, are a unique feature of GalE enzymes from Thermus species and important for activity as well as affinity
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
additional information
-
ligand binding structures, docking study, overview
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
-
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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
B1X789
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-tagatose
D-fructose
B1X789
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-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
C8VAU8
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
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Leloir pathway of membrane polysaccharide 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
-
-
?
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-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
-
-
r
UDP-galactose
UDP-glucose
-
role of the essential arginine residue in stretching and binding of the substrate
-
?
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
-
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
-
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
UDP-GlcNAc
UDP-GalNAc
-
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
additional information
?
-
-
Leloir pathway of galactose metabolism
-
-
?
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
?
-
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
?
-
-
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
?
-
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
-
additional information
?
-
-
no activity with UDP-N-acetylgalactoseamine
-
-
-
additional information
?
-
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
?
-
B1X789
no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
-
-
-
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
?
-
-
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 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
?
-
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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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
C8VAU8
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
-
Leloir pathway of membrane polysaccharide 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
-
-
?
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
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
-
-
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
Q9HDU3
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
?
-
-
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
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
?
-
-
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
-
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
?
-
-
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
?
-
Q9Y7X5
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
?
-
Q9Y7X5
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
NAD+
-
absolute requirement for NAD+. Km: 0.27 mM for the liver enzyme, Km: 0.28 mM for the mammary enzyme; Km: 0.29 mM for the thyroid enzyme
NAD+
Torulopsis candida
-
depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+
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+
-
two nicotinamide cofactors bind in symmetry-related positions in the dimer
NAD+
-
the amino acid side chains responsible for anchoring the NAD+ to the protein include Asp33, Asn37, Asp66, Tyr157 and Lys161
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+
-
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+
-
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+
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
additional information
an NAD+ binding motif is GGXGXXG, not required for activity
-
additional information
-
an NAD+ binding motif is GGXGXXG, not required for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
; 4 mM are included in assay medium; 4 mM are included in assay medium
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
galactose 6-phosphate
-
activation of minor enzyme form; partial inhibition of major enzyme form
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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
-
pH 8.9, 50°C, recombinant GalE; 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
-
enzyme shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate
-
additional information
additional information
Saccharomyces fragilis
-
classical hyperbolic kinetics with UDPgalactose, allosteric kinetics with UDPglucose
-
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
-
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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 (5–9 mM).
19
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5–9 mM).
24
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5–9 mM).
32
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5–9 mM).
33
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5–9 mM).
0.37
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
0.78
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
0.99
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
2.32
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
2.5
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
2.62
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
960
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
5.5
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
8.1
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
970
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
3400
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
103
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-glucose dehydrogenase
350
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-glucose dehydrogenase
397
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-glucose dehydrogenase
435
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
578
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 UDP-glucose dehydrogenase
0.78
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
0.79
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
46
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
232
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
1.55
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
3.13
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
5.39
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
5.43
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
5.92
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
6.61
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.6 - 12
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
5.6
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
Trypanosoma brucei
-
-
12
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
Homo sapiens
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.6
-
GALE activity evaluated in samples by monitoring the conversion of UDP-gal to UDP-glc. Assays stopped by the addition of 237.5 microliter of ice-cold water followed immediately by filtration through 0.2-micrometer nylon micro-spin columns (Corning) to remove proteins and particulates before high performance liquid chromatography analysis.
1.7
native protein, substrate is UDP-glucose; purified native enzyme, substrate UDP-Glc
4.6
purified recombinant detagged enzyme, substrate UDP-Glc; recombinant Pisum protein, substrate is UDP-glucose
16.7
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
19.8
native protein, substrate is UDP-galactose; purified native enzyme, substrate UDP-Gal
38.9
purified recombinant detagged enzyme, substrate UDP-D-Xyl; specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
49
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
53.3
purified recombinant detagged enzyme, substrate UDP-Gal; recombinant Pisum protein, substrate is UDP-galactose
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.3
-
activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3
8.6
8.7
9.5
8.6
assay at; assay at; assay at; assay at; assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6.7 - 8.1
-
6.7: 91% of maximal activity, 8.1: 88% of maximal activity
7 - 9.7
-
7: about 50% of maximal activity, 9.7: about 40% of maximal activity
6 - 9
pH 6.0: about 80% of maximal activit, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
levels of HvUGE1 mRNA are low in day 1 and day 3 coleoptiles, increases approximately 28fold in day 5 coleoptiles
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
expression of HvUGE1 is highest in leaf tips, rapidly decreases to very low levels in the basal region of the leaves
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
additional information
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
-
Heterodera schachtii parasitism strongly downregulates RDH1 expression in the root 3 days after inoculation
mRNA levels of HvUGE1 are very high in the maturation zone compared with other regions of the root
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
additional information
enzyme expression levels during different developmental stages evaluated by quantitative real-time reverse transcription PCR enzyme expression and immunohistochemic analysis, overview
additional information
-
enzyme expression levels during different developmental stages evaluated by quantitative real-time reverse transcription PCR enzyme expression and immunohistochemic analysis, overview
additional information
-
galE transcription exhibits a distinct expression profile under different culture conditions
additional information
-
galE transcription exhibits a distinct expression profile under different culture conditions
-