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UDP-alpha-D-glucose = UDP-alpha-D-galactose
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
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
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
-
-
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ADP-D-glucose
?
-
-
-
-
?
CDP-D-glucose
?
-
-
-
-
?
D-fructose
D-tagatose
-
-
-
?
D-galactose
D-glucose
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-glucose
D-galactose
-
-
-
?
D-psicose
D-sorbose
-
-
-
?
D-sorbose
D-psicose
-
-
-
?
D-tagatose
D-fructose
the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
-
-
?
Deoxy-UDP-D-glucose
?
-
-
-
-
?
TDP-6-deoxy-D-galactose
?
-
-
-
-
?
TDP-D-glucose
TDP-D-galactose
UDP-6-deoxy-D-glucose
?
-
-
-
-
?
UDP-6-deoxygalactose
UDP-6-deoxyglucose
-
-
-
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
UDP-alpha-D-glucose
UDP-alpha-D-galactose
UDP-D-galactose-hexodialose
?
-
-
-
-
?
UDP-D-glucose
UDP-D-galactose
UDP-D-xylose
UDP-L-arabinose
UDP-galactose
UDP-glucose
UDP-glucose
UDP-galactose
UDP-L-arabinose
?
-
-
-
-
?
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-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
-
-
-
?
additional information
?
-
TDP-D-glucose

TDP-D-galactose
-
-
-
?
TDP-D-glucose
TDP-D-galactose
-
-
-
?
UDP-alpha-D-galactose

UDP-alpha-D-glucose
-
-
-
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
-
-
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
-
-
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
-
-
-
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
-
-
r
UDP-alpha-D-glucose

UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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
Q81JK4, Q81K34
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
reaction mechanism modelling, overview
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
anthocyanin biosynthesis
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
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
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-alpha-D-glucose
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
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-alpha-D-glucose
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
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
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
-
-
-
-
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
-
-
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
-
-
-
-
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
-
-
-
-
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-glucose
UDP-D-galactose
-
carbohydrate biosynthesis
-
-
r
UDP-D-glucose
UDP-D-galactose
-
carbohydrate catabolism
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
r
UDP-D-xylose

UDP-L-arabinose
-
-
-
r
UDP-D-xylose
UDP-L-arabinose
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-Gal

UDP-Glc
-
-
-
r
UDP-Gal
UDP-Glc
-
-
-
-
r
UDP-galactose

UDP-glucose
-
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
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
-
-
-
?
UDP-galactose
UDP-glucose
Q81JK4, Q81K34
-
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
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
-
glycolysis and TCA cycle, Leloir pathway
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
r
UDP-galactose
UDP-glucose
-
-
?
UDP-galactose
UDP-glucose
-
-
?
UDP-galactose
UDP-glucose
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
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
-
galactose metabolic pathway
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
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
-
final step of the Leloir pathway
-
-
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
-
-
-
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
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
?
UDP-galactose
UDP-glucose
-
-
-
r
UDP-galactose
UDP-glucose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
r
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
Leloir pathway of D-galactose catabolism
-
-
?
UDP-galactose
UDP-glucose
-
Leloir pathway of galactose metabolism
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
-
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
r
-
?
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
r
-
?
UDP-galactose
UDP-glucose
glycolysis and TCA cycle, Leloir pathway
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
UDP-galactose
UDP-glucose
-
-
-
-
r
UDP-galactose
UDP-glucose
Torulopsis candida
-
-
-
?
UDP-galactose
UDP-glucose
Trigonella sp.
-
-
-
?
UDP-galactose
UDP-glucose
-
r
-
?
UDP-galactose
UDP-glucose
-
-
-
?
UDP-GalNAc

UDP-GlcNAc
-
-
-
-
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
-
-
-
-
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-GalNAc
UDP-GlcNAc
-
-
-
?
UDP-GalNAc
UDP-GlcNAc
-
-
-
r
UDP-GalNAc
UDP-GlcNAc
-
-
-
-
?
UDP-Glc

UDP-Gal
-
-
-
-
r
UDP-Glc
UDP-Gal
-
-
-
-
r
UDP-Glc
UDP-Gal
-
-
-
-
r
UDP-GlcNAc

UDP-GalNAc
-
-
-
-
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
UDP-GlcNAc
UDP-GalNAc
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
-
-
-
r
UDP-glucose

UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
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
-
-
?
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
?
-
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
?
-
-
enzyme of 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 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
?
-
xylose-inducible gene
-
-
?
additional information
?
-
-
xylose-inducible gene
-
-
?
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
?
-
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
?
-
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, 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
?
-
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose
UDP-alpha-D-galactose
UDP-D-glucose
UDP-D-galactose
UDP-D-xylose
UDP-L-arabinose
-
-
-
r
UDP-galactose
UDP-glucose
UDP-glucose
UDP-galactose
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
additional information
?
-
UDP-alpha-D-glucose

UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
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
Q81JK4, Q81K34
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
anthocyanin biosynthesis
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
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-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
-
-
-
r
UDP-D-glucose

UDP-D-galactose
-
-
-
r
UDP-D-glucose
UDP-D-galactose
-
carbohydrate biosynthesis
-
-
r
UDP-D-glucose
UDP-D-galactose
-
carbohydrate catabolism
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
r
UDP-galactose

UDP-glucose
-
-
-
-
r
UDP-galactose
UDP-glucose
Q81JK4, Q81K34
-
-
-
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
-
glycolysis and TCA cycle, Leloir pathway
-
-
?
UDP-galactose
UDP-glucose
-
enzyme catalyzes the first step of the Lelpoir pathway
-
-
r
UDP-galactose
UDP-glucose
-
galactose metabolic 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
-
final step of the Leloir pathway
-
-
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
-
-
-
r
UDP-galactose
UDP-glucose
-
-
-
?
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-galactose
UDP-glucose
-
-
-
-
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-Glc

UDP-Gal
-
-
-
-
r
UDP-Glc
UDP-Gal
-
-
-
-
r
UDP-GlcNAc

UDP-GalNAc
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
-
-
-
-
r
UDP-glucose

UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
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
?
-
-
enzyme of galactose metabolism
-
-
?
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
?
-
xylose-inducible gene
-
-
?
additional information
?
-
-
xylose-inducible gene
-
-
?
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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NADH
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
NAD+

-
-
NAD+
Torulopsis candida
-
depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+
NAD+
-
no requirement for external NAD+
NAD+
-
Km: 0.29 mM for the thyroid enzyme
NAD+
-
contains one molecule of NAD+ per dimer
NAD+
-
exogenous NAD+ is not required for activity, but removal causes inactivation
NAD+
-
not dependent on addition of NAD+
NAD+
-
contains firmly bound NAD+
NAD+
-
each dimer contains one molecule of NAD+ tightly bound
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+
-
one mol firmly bound per dimer
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+
-
is particularly important
NAD+
non-covalently bound, required in bacteria
NAD+
-
bound to the enzyme via GxxGxxG motif
NAD+
-
bound to the enzyme via GxxGxxG motif
NAD+
-
one ligand bound per subunit
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+
associated to enzyme residue Lys150
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
-
additional information
Q81JK4
contains an NAD+ binding site
-
additional information
Q81K34
contains an NAD+ binding site
-
additional information
-
contains an NAD+ binding site
-
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1,2-Cyclohexanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2',3'-O-(2,4,6-Trinitrocyclohexadienylidene)uridine 5'-monophosphate
-
powerful reversible inhibitor
2,3-Butanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
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
5-(adenosine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
5-(thymidine-5'-diphosphoryl)-D-glucose
-
reductive inhibition
5-(Thymidine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
Cu2+
5 mM, 95% loss of activity
D-galactose
Torulopsis candida
-
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
Dimethylsulfoxide
10%, 26% inhibition
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
Hg2+
complete inhibition, recombinan t enzyme
L-Arabinose plus UMP or UDP
-
L-Xylose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
methanol
10%, 26% inhibition
NaBH4
-
reductive inhibition
NADPH
-
very weak inhibitory effect
p-hydroxymercuribenzoate
-
-
P1-5'-Uridine-P2-glucose-6-yl diphosphate
-
-
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
Phenylglyoxal
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
Salt
-
moderately inhibited by high salt concentrations
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
Thymidine diphospho-6-deoxy-D-xylo-4-hexosulose
-
reductive inhibition
-
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
UDP-N-acetylgalactosamine
competitive, binding study
UDP-N-acetylglucosamine
competitive, binding study
Uridine 5'-diphosphate bromoacetol
-
-
Uridine 5'-diphosphate chloroacetol
-
-
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
5'-UMP

-
-
5'-UMP
-
strong, competitive
5'-UMP
-
strong, 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
-
strong, competitive
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
5'-UMP
Saccharomyces fragilis
-
-
5'-UMP
Torulopsis candida
-
-
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
diethylstilbestrol

-
-
ebselen

-
-
Ethacrynic acid

-
-
galactose 6-phosphate

-
activation of the minor enzyme form
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
-
glucose plus UMP
Torulopsis candida
-
-
-
haloprogin

-
-
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
-
reductive inhibition
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

-
slightly inhibiting
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
NEM

-
-
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
no inactivation by p-chloromercuribenzoate
p-chloromercuribenzoate
-
-
psammaplin A

-
-
UDP

-
-
UDP
-
5.0 mM, 25% inhibition
UMP

-
UMP
-
5.0 mM, 44% inhibition
UTP

-
slightly
UTP
-
5.0 mM, 13% inhibition
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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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.
Down Syndrome
UDP-galactose-4-epimerase in a boy with a trisomy 21.
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
Epimerase-deficiency galactosemia is not a binary condition.
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
Galactose Epimerase Deficiency: Expanding the Phenotype.
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
In vivo and in vitro function of human UDP-galactose 4'-epimerase variants.
Galactosemias
In vivo metabolism and UTP-depleting action of 2-deoxy-2-fluoro-D-galactose.
Galactosemias
Issues on universal screening for 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
Structure modeling and comparative genomics for epimerase enzyme (Gal10p).
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 galactosemia - Past, present and future.
Galactosemias
The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients.
Galactosemias
The structural and molecular biology of type III galactosemia.
Galactosemias
[Effectiveness of the screening programme for galactosemia. New strategy in Poland]
Galactosemias
[UDP-galactose-4-epimerase deficiency]
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.
Genetic Diseases, Inborn
The structural and molecular biology of type III galactosemia.
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.
Neoplasms
Sequence-dependent variations associated with H2A/H2B depletion of nucleosomes.
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.
udp-glucose 4-epimerase deficiency
[UDP-galactose-4-epimerase deficiency]
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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26.4
D-galactose
in McIlvaine buffer (pH 7.5), at 35°C
2 - 37
D-tagatose
in McIlvaine buffer (pH 7.5), at 35°C
0.23 - 12.9
UDP-alpha-D-galactose
0.06 - 260
UDP-alpha-D-glucose
0.057 - 0.29
UDP-D-galactose
0.31
UDP-D-glucose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.15
UDP-D-xylose
pH 8.6, 25°C
0.035 - 3.9
UDP-galactose
0.16
UDP-L-arabinose
pH 8.6, 25°C
1.06
UDP-N-acetyl-alpha-D-galactosamine
pH 7.0, 80°C
0.146 - 2.4
UDP-N-acetyl-alpha-D-glucosamine
0.15
UDP-xylose
pH 8.6, 25°C
0.0083 - 1.67
UDPgalactose
additional information
additional information
-
0.23
UDP-alpha-D-galactose

pH 6.5, 60°C
5.53
UDP-alpha-D-galactose
pH 7.0, 80°C
12.9
UDP-alpha-D-galactose
recombinant enzyme, pH 7.0, 80°C
0.06
UDP-alpha-D-glucose

mutant L320Y, pH 8.5, 25°C
0.1 - 1
UDP-alpha-D-glucose
wild-type enzyme, pH 8.5, 25°C
2 - 6
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
2.24
UDP-alpha-D-glucose
pH 6.5, 60°C
5.53
UDP-alpha-D-glucose
recombinant enzyme, pH 7.0, 80°C
12.9
UDP-alpha-D-glucose
pH 7.0, 80°C
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
0.04
UDP-Gal

-
0.035
UDP-galactose

-
37°C, pH 8.8, mutant enzyme L313M
0.04
UDP-galactose
pH 8.0, 25°C
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
0.066
UDP-galactose
-
37°C, pH 8.8, mutant enzyme K257R
0.069
UDP-galactose
-
37°C, pH 8.8, wild-type enzyme
0.078
UDP-galactose
-
37°C, pH 8.8, mutant enzyme G319E
0.082
UDP-galactose
-
37°C, pH 8.8, mutant enzyme N34S
0.093
UDP-galactose
-
37°C, pH 8.8, mutant enzyme G90E
0.097
UDP-galactose
-
37°C, pH 8.8, mutant enzyme L183P
0.099
UDP-galactose
-
37°C, pH 8.8, mutant enzyme R335H
0.1 - 0.13
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.11
UDP-galactose
-
25°C, pH 8.8
0.14
UDP-galactose
-
37°C, pH 8.8, mutant enzyme D103G
0.16
UDP-galactose
-
24°C, pH 7.0
0.16
UDP-galactose
-
37°C, pH 8.8, mutant enzyme V94M
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
0.255
UDP-galactose
in McIlvaine buffer (pH 7.5), at 35°C
0.258
UDP-galactose
-
pH 8.9, 50°C, recombinant GalE
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
0.29
UDP-galactose
pH 8.6, 25°C
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
0.784
UDP-galactose
-
37°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
3.9
UDP-galactose
in 100 mM MES-NaOH (pH 5.5), at 70°C
0.16
UDP-GalNAc

-
0.16
UDP-GalNAc
pH 8.0, 25°C
0.055
UDP-Glc

-
0.2
UDP-GlcNAc

-
0.2
UDP-GlcNAc
pH 8.0, 25°C
0.055
UDP-glucose

pH 8.0, 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
0.31
UDP-glucose
pH 8.6, 25°C
0.56
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.76
UDP-glucose
-
values are indirectly determined from the Haldane relationship
1.2
UDP-glucose
-
24°C, pH 7.0
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
2.4
UDP-N-acetyl-alpha-D-glucosamine
pH 7.0, 80°C
0.0083
UDPgalactose

-
mammary enzyme
0.017
UDPgalactose
-
liver enzyme
0.026
UDPgalactose
-
mutant Y149F
0.048
UDPgalactose
-
mutant S124A
0.1
UDPgalactose
-
native and renatured enzyme
0.12
UDPgalactose
Saccharomyces fragilis
-
-
0.14
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
0.18
UDPgalactose
-
native and renatured enzyme
0.225
UDPgalactose
-
wild type enzyme
0.256
UDPgalactose
-
mutant S124T
1.2
UDPgalactose
Torulopsis candida
-
-
0.25
UDPglucose

-
-
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
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00026
D-galactose
in McIlvaine buffer (pH 7.5), at 35°C
0.00545
D-tagatose
in McIlvaine buffer (pH 7.5), at 35°C
1 - 14677
UDP-alpha-D-galactose
0.073 - 14677
UDP-alpha-D-glucose
17
UDP-D-xylose
pH 8.6, 25°C
0.046 - 750
UDP-galactose
23
UDP-L-arabinose
pH 8.6, 25°C
38295
UDP-N-acetyl-alpha-D-galactosamine
pH 7.0, 80°C
0.37 - 27671
UDP-N-acetyl-alpha-D-glucosamine
17
UDP-xylose
pH 8.6, 25°C
1
UDP-alpha-D-galactose

pH 6.5, 60°C
7757
UDP-alpha-D-galactose
pH 7.0, 80°C
14677
UDP-alpha-D-galactose
recombinant enzyme, pH 7.0, 80°C
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
1.1
UDP-alpha-D-glucose
pH 6.5, 60°C
1.5
UDP-alpha-D-glucose
mutant L320Y, pH 8.5, 25°C
12.8
UDP-alpha-D-glucose
wild-type enzyme, pH 8.5, 25°C
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
7757
UDP-alpha-D-glucose
recombinant enzyme, pH 7.0, 80°C
14677
UDP-alpha-D-glucose
pH 7.0, 80°C
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
0.046
UDP-galactose

-
37°C, pH 8.8, mutant enzyme G90E
0.633
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
0.84
UDP-galactose
in 100 mM MES-NaOH (pH 5.5), at 70°C
1.1
UDP-galactose
-
37°C, pH 8.8, mutant enzyme V94M
5
UDP-galactose
-
37°C, pH 8.8, mutant enzyme D103G
5.1
UDP-galactose
-
37°C, pH 8.8, mutant enzyme K257R
5.8
UDP-galactose
-
37°C, pH 8.8, mutant enzyme L313M
11
UDP-galactose
-
37°C, pH 8.8, mutant enzyme L183P
15
UDP-galactose
-
37°C, pH 8.8, mutant enzyme R335H
21
UDP-galactose
25°C, pH 8.0
23 - 24
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
28 - 34
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
30
UDP-galactose
-
37°C, pH 8.8, mutant enzyme G319E
32
UDP-galactose
-
37°C, pH 8.8, mutant enzyme N34S
36
UDP-galactose
-
37°C, pH 8.8, wild-type enzyme
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
55.32
UDP-galactose
-
pH 8.9, 50°C, recombinant GalE
64
UDP-galactose
pH 8.6, 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
290.1
UDP-galactose
-
37°C
500
UDP-galactose
-
24°C, pH 7.0
750
UDP-galactose
in McIlvaine buffer (pH 7.5), at 35°C
0.12
UDP-GalNAc

25°C, pH 8.0
0.07
UDP-GlcNAc

25°C, pH 8.0
2 - 8
UDP-glucose

-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5â9 mM).
9
UDP-glucose
pH 8.6, 25°C
11
UDP-glucose
25°C, pH 8.0
18
UDP-glucose
-
24°C, pH 7.0
19
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (5â9 mM).