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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
-
-
?
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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
-
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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 (59 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 (59 mM).
24
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
32
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
33
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 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
27671
UDP-N-acetyl-alpha-D-glucosamine
pH 7.0, 80°C
0.073
UDPgalactose
-
mutant Y149F
0.265
UDPgalactose
-
,mutant S124A
248
UDPgalactose
-
mutant S124T
760
UDPgalactose
-
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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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
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure
evolution
bifunctional UDP-glucose 4-epimerases, UGEs, with UDP-xylose 4-epimerase (EC 5.1.3.5) activity are conserved in vascular plants
evolution
presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
evolution
sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
evolution
the rice genome contains four putative UGE-encoding genes (OsUGE1-4). All four predicted OsUGEs in rice carry an epimerase domain and belong to the NAD+ dependent epimerase/dehydratase family proteins that use NAD+ as a cofactor and nucleotide-sugars as substrates. Expression profiles of UGEs in Oryza sativa support distinct in planta roles throughout development
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa). Despite the relatively low sequence identity among all three groups, the similarity of the enzymes' tertiary structures is striking with an overall RMSD of the multiple structure alignment being 1.08 A and variation being most pronounced at the C-terminal end
evolution
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
evolution
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
evolution
the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
evolution
-
the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
-
evolution
-
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
-
evolution
-
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
-
evolution
-
sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
-
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
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
-
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
-
evolution
-
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
-
evolution
-
presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
-
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
-
a Xcc galE mutant has reduced biofilm formation ability
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
enzyme overexpressing mutant OsUGE1-OX lines maintain 18-24% more sucrose and 12-22% less cellulose in shoots compared to wild-type when subjected to suboptimal N-levels. OsUGE1-OX lines maintain proportionally more galactose and glucose in the hemicellulosic polysaccharide profile of plants compared to wild-type plants when grown under low N. The altered cell wall C-partitioning during N-limitation in the OsUGE1-OX lines appears to be mediated by OsUGE1 via the repression of the cellulose synthesis associated genes, OsSus1, OsCesA4, 7, and 9. OsUGE1 shows phenotypic alteration at carbohydrate partitioning level in the transgenic lines, overexpressinon phenotypes, overview
malfunction
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
malfunction
mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
malfunction
mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
malfunction
silencing GALE gene with specific siRNAs results in a markedly inhibition of proteoglycans (PGs)synthesis in human articular chondrocytes. GALE protein levels are also decreased in both human osteoarthritis cartilage, thus leading to losses of PGs contents. GALE inhibition might contribute to osteoarthritis progress. Mutations of gene GALE in humans results in an inherited metabolic disease, the type III galactosemia
malfunction
the replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
malfunction
the S306Y mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
malfunction
-
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
-
malfunction
-
mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
-
malfunction
-
a Xcc galE mutant has reduced biofilm formation ability
-
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
-
the replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
-
malfunction
-
mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
-
metabolism
-
GALE catalyzes the third step of the Leloir pathway of galactose metabolism
metabolism
GALE is involved in the galactose metabolic pathway
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
the enzyme is involved in D-galactose metabolism
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
-
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
-
metabolism
-
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
-
metabolism
-
the enzyme is involved in D-galactose metabolism
-
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 enzyme is involved in D-galactose metabolism
-
metabolism
-
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
-
physiological function
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
-
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
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
-
galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
-
GalE plays a key role in lipopolysaccharide biosynthesis
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
-
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
enzyme OsUGE1 plays an important role in carbohydrate partitioning to the cell wall in Oryza sativa
physiological function
enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UGE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UGE is important in the composition of the sugar nucleotide pools
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UXE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UXE is important in the composition of the sugar nucleotide pools
physiological function
UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
physiological function
UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
physiological function
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
physiological function
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The 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
physiological function
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The 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
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of other polysaccharide structures, such as capsular polysaccharide (CPS), or extracellular polysaccharide (EPS) from Streptococcus thermophilus, one of the most widely used bacteria in the dairy industry
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of other polysaccharide structures, such as proteoglycans (PGs) of articular chondrocytes. Secondary role of the human enzyme is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc)
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures, such as capsular polysaccharide (CPS)
physiological function
UDP-galactose 4-epimerase plays an essential role in development and homeostasis of Drosophila that extends beyond the Leloir pathway. UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose-4-epimerase (GALE) is a key enzyme catalyzing the interconversion of UDP-glucose and UDP-galactose, as well as UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine, which are all precursors for the proteoglycans (PGs) synthesis. Role of GALE in PGs synthesis of human articular chondrocytes, the GALE expression in osteoarthritis, and the regulation of GALE expression by interleukin-1beta, overview. GALE mRNA expression is stimulated by interleukin-1beta in early phase, but suppressed in late phase, while the suppression of GALE expression induced by interleukin-1beta is mainly mediated by stress-activated protein kinase/c-Jun N-terminal kinase pathway. Both SAP/JNK inhibitor SP600125 and p38 MAPK inhibitor SB203580 attenuate the suppression of interleukin-1beta on GAG synthesis and GALE mRNA expression of chondrocyte. Critical role of GALE in maintaining cartilage homeostasis
physiological function
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
physiological function
-
UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
-
physiological function
-
UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
-
physiological function
-
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The 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
-
physiological function
-
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The 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
-
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
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
physiological function
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
-
enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
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additional information
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homology structural modeling, overview
additional information
ligand binding structures, docking study, overview
additional information
-
ligand binding structures, docking study, overview
additional information
-
ligand-bound enzyme structures, active site structure including Lys153, Tyr149, and Ser124, overview
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
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
comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
additional information
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
additional information
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
additional information
-
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
additional information
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
additional information
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dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
additional information
enzyme structure and substrate specificity, structure-function relationship, overview. Comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes
additional information
Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
additional information
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
-
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
-
comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
-
additional information
-
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
-
additional information
-
Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
-
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
-
additional information
-
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
-
additional information
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homology structural modeling, overview
-
additional information
-
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
-
additional information
-
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
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x * 40600, recombinant plasmid-expressed UgeA, SDS-PAGE
?
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x * 35400, calculation from nucleotide sequence
?
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x * 38266, calculation from nucleotide sequence
?
x * 39000, recombinant enzyme, SDS-PAGE
?
-
x * 38994, calculation from nucleotide sequence
?
x * 38000, about, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 38000, about, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 37000, calculation from nucleotide sequence
?
-
x * 42213, sequence calculation
?
-
x * 42213, sequence calculation
-
dimer
-
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
dimer
-
2 * 38800, gel filtration
dimer
-
fully active enzyme
dimer
-
2 * 38800, gel filtration
-
dimer
-
2 * 42000, SDS-PAGE
dimer
-
wild-type protein and all the mutants (N34S, G90E, V94M, D103G, L183P, K257R, L313M, G319E and R335H) are able to form dimers. In all cases, especially with the mutant proteins, some higher molecular mass species are also observed
dimer
homodimer, 2 * 39000
dimer
-
homodimer, 2 * 39000
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 60000, enzyme exists in an active dimeric and an active tetrameric form
dimer
-
2 * 59000, SDS-PAGE
dimer
-
2 * 78000, SDS-PAGE
dimer
-
2 * 78000, SDS-PAGE
-
dimer
-
The resulting model is composed of four subunits forming two physiological dimers (subunits AB and CD). Subunit A comprises residues -1150, 157237 and 249381, subunit B residues -1150, 158235 and 249381, subunit C residues -1152, 158237 and 248381 and subunit D residues -1150, 157235 and 249381.The -1 refers to a serine residue which precedes the initiating methionine and is an artifact of the expression plasmid that generates an N-terminal extension. There are several missing residues which belong to flexible surface loops. Each active site is occupied by well ordered NAD+ and UDP-FGal.
hexamer
enzyme Ab-WbjB is a hexamer, organised into a trimer of chain pairs, with coenzyme NADP+ occupying each chain
hexamer
-
enzyme Ab-WbjB is a hexamer, organised into a trimer of chain pairs, with coenzyme NADP+ occupying each chain
-
homodimer
-
a homodimer, containing one catalytic site and one NAD+ as cofactor per subunit, not showing fast association-dissociation
homodimer
2 * 32000, SDS-PAGE
homodimer
2 * 35000, SDS-PAGE
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
2 * 35000, SDS-PAGE
homodimer
2 * 34899, calculated from sequence
homodimer
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
-
2 * 34899, calculated from sequence
-
homodimer
-
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
-
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
-
2 * 34899, calculated from sequence
-
homodimer
-
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
-
monomer
-
-
monomer
-
2 * 36700, SDS-PAGE
monomer
-
2 * 37100, SDS-PAGE
monomer
-
2 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
monomer
-
1 * 39000, subunits of the dimeric epimerase are stabilized under certain conditions where they can function catalytically
tetramer
-
-
tetramer
-
4 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
tetramer
-
4 * 60000, enzyme exists in an active dimeric and an active tetrameric form
additional information
-
homology structural modeling, overview
additional information
-
homology structural modeling, overview
-
additional information
-
nucleotide sequence
additional information
the enzyme has an N-terminal nucleotide binding domain and a smaller C-terminal domain that is responsible for the correct positioning of its substrate, a UDP-sugar. The N-terminal domain comprises seven parallel beta-strands that are flanked on both sides by alpha-helices and shape the Rossmann fold. Two paired Rossmann folds tightly bind one NAD+ cofactor per subunit
additional information
determination of the structure of human UDP-Gal 4-epimerase. The C-terminal domain is built from five beta-strands and four alpha-helices
additional information
-
determination of the structure of human UDP-Gal 4-epimerase. The C-terminal domain is built from five beta-strands and four alpha-helices
additional information
-
sequence comparisons and structure homology modeling, overview. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine
additional information
enzyme secondary structure analysis using circular dichroism
additional information
-
enzyme secondary structure analysis using circular dichroism
-
additional information
nucleotide sequence
additional information
-
nucleotide sequence
additional information
enzyme structure analysis, overview
additional information
-
enzyme structure analysis, overview
additional information
-
enzyme structure analysis, overview
-
additional information
-
enzyme structure analysis, overview
-
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M134A
site-directed mutagenesis
M134Y
site-directed mutagenesis
M134A
-
site-directed mutagenesis
-
M134Y
-
site-directed mutagenesis
-
K153N
-
the mutation affects the catalytic activity only slightly, however, the NAD+ binding potential is reduced dramatically
Y149G
-
the mutant is completely inactive
Y149G/K153N
-
the mutant is completely inactive
K160V
site-directed mutagenesis of the key residue responsible for anchoring of the co-factor, inactive mutant
L320C
site-directed mutagenesis of a gate-keeper residue, the L320C mutant enzyme is also active in UDPGlcpNAc/UDP-GalpNAc interconversion
L320Y
site-directed mutagenesis of a gate-keeper residue, the L320Y mutant enzyme is not active in UDPGlcpNAc/UDP-GalpNAc interconversion
Y156F
site-directed mutagenesis of the key residue serving as the active site base, inactive mutant
K153A
-
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. 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
N179S
the 4-epimerization of tagatose is enhanced 2fold in this mutant
S124A/Y229F
site-directed mutagenesis, inactive mutant
S143A
site-directed mutagenesis, the mutation abolishes activity on non-acetylated substrates, probably due to loss of the hydrogen bonding, whereas the mutant remains active on UDP-GlcNAc/UDP-GalNAc, as additional stabilizing interactions with the N-acetyl moiety are present
S144K
site-directed mutagenesis, inactive mutant
S306Y
-
plasmid containing the Gne S306Y constructed using the QuikChange Site-Directed Mutagenesis kit (Stratagene, La Jolla, CA).The S306Y mutation totally abolished activity toward the acetylated substrate.
-
A25V
the mutant shows reduced activity compared to the wild-type enzyme
C307Y
-
normal activity with respect to UDP-galactose, complete loss of activity with respect to UDP-N-acetylgalactosamine
D69E
the mutant shows reduced activity compared to the wild-type enzyme
G302D
the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
G319E
-
very littel change in steady-state kinetic parameters compared with the wild-type protein
K257R
-
the ratio of turnover number to Km-value is 6.7fold lower than the wild-type ratio
L313M
-
the ratio of turnover number to Km-value is 3.0fold lower than the wild-type ratio
M284K
-
the mutant is active in vivo, but not in vitro and shows reduced enzymatic activity (1.1% residual activity) and reduced stability towards denaturants in vitro
N268D
-
the mutant demonstrates 63% residual activity
R169W
the mutant shows reduced activity compared to the wild-type enzyme
R239W
the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
R40C
the mutant shows reduced activity compared to the wild-type enzyme
S132A
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
S132A/Y157F
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
Y105C
-
the mutant demonstrates 13% residual activity
Y157F
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
G118A/G119A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
G188S/G119S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S116A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S279Y
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
T117S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
K150R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
S121A
site-directed mutagenesis, inactive mutant
Y146F
site-directed mutagenesis, inactive mutant
K150R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
-
S121A
-
site-directed mutagenesis, inactive mutant
-
Y146F
-
site-directed mutagenesis, inactive mutant
-
C300Y
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
K86G
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
C300Y
-
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
-
K86G
-
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
-
K151A
-
site-directed mutagenesis, inactive mutant
S123A
-
site-directed mutagenesis, inactive mutant
Y147A
-
site-directed mutagenesis, almost inactive mutant
K151A
-
site-directed mutagenesis, inactive mutant
-
S123A
-
site-directed mutagenesis, inactive mutant
-
Y147A
-
site-directed mutagenesis, almost inactive mutant
-
N191D
naturally occuring mutation, the UgeA mutant shows reduced galactofuranose production, the mutant enzyme is partially active
N191D
-
naturally occuring mutation, the UgeA mutant shows reduced galactofuranose production, the mutant enzyme is partially active
-
K153M
-
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. 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
K153M
mutation results in a 13C chemical shift of 150.8 ppm, which is 0.9 ppm downfield from that of wild-type and 1.8 ppm upfield from that of Y149F epimerase
K153M
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
S124A
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124A
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S124A
site-directed mutagenesis
S124A
-
in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. Epimerization proceeds with a deuterium kinetic isotope effect of about 2 throughout the pH range 6.3-9.0
S124A
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
S124A/Y149F
-
epimerization proceeds at a turnover number that is lower by a factor of 10000000 than that of the wild-type enzyme. This is attributed to the synergistic action of Tyr149 and Ser124 in wild-type enzyme and to the absence of any internal catalysis of hydride transfer in the doubly mutated enzyme. 80% inactivation after 8 min at 50°C compared to 20% inactivation of the wild-type enzyme
S124A/Y149F
mutation causes a 13C downfield perturbation of 2.8 ppm to 152.7 ppm
S124T
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124T
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S124T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S124V
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124V
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S306Y
-
plasmid containing the Gne S306Y constructed using the QuikChange Site-Directed Mutagenesis kit (Stratagene, La Jolla, CA).The S306Y mutation totally abolished activity toward the acetylated substrate.
S306Y
site-directed mutagenesis, the mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates,which results in the observed loss of activity
Y149F
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values form Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
Y149F
-
in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. At pH there is no significant isotope effect, but at pH 6.3, the isotope effect is 2.2
Y149F
mutation results in a 13C downfield perturbation of 2.7 ppm to 152.6 ppm
Y149F
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
Y299C
-
mutation results in a loss of epimerase activity with regard to UDPgalactose by almost 5fold, it results in a gain of activity against UDP-GalNAc by more than 230fold
Y299C
site-directed mutagenesis, structure analysis in complex with UDP-N-acetylglucosamine, PDB ID 1LRK, the Y299C mutation in eGalE results in significant loss of activity on non-acetylated substrates
D103G
-
the ratio of turnover number to Km-value is 14.4fold lower than the wild-type ratio
D103G
-
the mutant demonstrates 82.1% residual activity
G90E
-
the ratio of turnover number to Km-value is 1040fold lower than the wild-type ratio. Mutant enzyme is more susceptible to proteolysis than the wild-type protein, presence of substrate at saturating level (1 mM) partially protect the enzyme from proteolysis
G90E
-
the mutant demonstrates 1% residual activity
L183P
-
the ratio of turnover number to Km-value is 4.7fold lower than the wild-type ratio. Mutant enzyme is highly susceptible to proteolysis during expression and purification
L183P
-
the mutant demonstrates 3.3% residual activity
N34S
-
very little change in steady-state kinetic parameters compared with the wild-type protein. Mutant enzyme is more susceptible to proteolysis than the wild-type protein, presence of substrate at saturating level (1 mM) partially protect the enzyme from proteolysis
N34S
-
the mutant demonstrates above 65.1% residual activity
R335H
-
the ratio of turnover number to KM-value is 3.5fold lower than the wild-type ratio
R335H
the mutant shows reduced activity compared to the wild-type enzyme
V94M
-
the ratio of turnover number to Km-value is 75fold lower than the wild-type ratio
V94M
-
the mutant demonstrates 2.6% residual activity
additional information
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
additional information
-
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
additional information
-
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
-
additional information
-
generation of single disruption mutants and DELTAuge3 DELTAuge5 double mutant, phenotypes, overview
additional information
-
generation of single disruption mutants and DELTAuge3 DELTAuge5 double mutant, phenotypes, overview
-
additional information
-
a ugeADELTA knockout strain is viable, but has defects including wide, slow growing, highly branched hyphae and reduced conidiation. ugeADELTA colonies have substantially reduced sporulation but normal spore viability. Conidia of the ugeADELTA strain can not form colonies on galactose as a sole carbon source, however they produced short, multinucleate germlings, suggesting they ceased to grow from starvation
additional information
targeted deletion of ugeA resulting in a severe reduction of galactofuranose in N-linked glucans
additional information
-
targeted deletion of ugeA resulting in a severe reduction of galactofuranose in N-linked glucans
-
additional information
-
second-order rate constants for reductive inactivation of wild-type and mutant epimerases, overview
additional information
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
-
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
addition of NAD+ to Lys150 significantly abrogates the loss of activity. None of the mutations affected the quaternary structure of the protein
additional information
-
addition of NAD+ to Lys150 significantly abrogates the loss of activity. None of the mutations affected the quaternary structure of the protein
-
additional information
development of transgenic rice plants to constitutively overexpress the OsUGE-1 gene (OsUGE1-OX1-2). The transgenic rice lines are similar in size to wild-type plants at the vegetative stage and at maturity regardless of the N-level tested. OsUGE1-OX lines maintain 18-24% more sucrose and 12-22% less cellulose in shoots compared to wild-type when subjected to suboptimal N-levels. OsUGE1-OX lines maintain proportionally more galactose and glucose in the hemicellulosic polysaccharide profile of plants compared to wild-type plants when grown under low N. The altered cell wall C-partitioning during N-limitation in the OsUGE1-OX lines appears to be mediated by OsUGE1 via the repression of the cellulose synthesis associated genes, OsSus1, OsCesA4, 7, and 9. Seed characteristics of rice plants overexpressing OsUGE1 compared to wild-type rice, overview
additional information
a GalE loop deletion mutant (mut1), in which residues 32-43 (NLSSGRREFVNP) of the NAD-binding loop are replaced with residues 33-40 (IVQRDTGG) of the corresponding loop from Thermoplasma volcanium binds NAD+ in a loose, reversible manner
additional information
-
a GalE loop deletion mutant (mut1), in which residues 32-43 (NLSSGRREFVNP) of the NAD-binding loop are replaced with residues 33-40 (IVQRDTGG) of the corresponding loop from Thermoplasma volcanium binds NAD+ in a loose, reversible manner
additional information
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
additional information
-
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
additional information
-
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
-
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DNA and amino acid sequence determination and analysis, quantitative real-time reverse transcription PCR enzyme expression analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli Rosetta cells and in a gal10-null strain of Saccharomyces cerevisiae strain JFy3835
-
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli and Saccharomyces cerevisiae
-
expression in GALE-null line of Chineses hamster ovary cells. GALE-null cells accumulats abnormally high levels of Hal-1-P and UDP-Gal and abnormally low levels of UDP-Glc and UDP-GLcNAc in the presence of galactose. Human GALE expression corrects each of theses defects
-
expression in GALE-null line of Chinesese hamster ovary cells. Enzyme from Escherichia coli can not restore the metabolic balance, because unlike the mammalian enzyme it can not catalyze the interconversion of UDP-GalNAc and UDP-GlcNAc
-
expression in in Escherichia coli
expression in Pichia pastoris
-
Expression in Saccharomyces cerevisiae EBY100.
-
expression in Sinorhizobium meliloti
-
expression of GFP-tagged wild-type enzyme in HEK-293T cells, and transient expression of myc-tagged GALER239W and GALEG302D, and of myc- or FLAG-tagged GALE165K and GALEW336X in HEK-293T cells and in GALE-null ldlD cells
expression of His-tagged enzyme
-
expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold
expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
galE transcription exhibits a distinct expressionprofile under different culture conditions, mapping of galE transcription initiation
-
gene BAS5114, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
Q81JK4, Q81K34
gene fnlA or ABD1_580, DNA and amino acid sequence determination and analysis, sequence comparisons, the gene belongs to the components of polysaccharide biosynthesis cluster RGP01, overview, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
gene galE, functional expression of N-termminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene GALE, real-time quantitative PCR expression analysis in chondrocytes
gene galE, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and functional complementation of enzyme-deficient Escherichia coli strain BW25113 DELTAgalE
gene galE-1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene galE1 or Rv3634c, sequence comparisons, e.g. with the enzyme from Mycobacterium smegmatis strain mc2 4517, recombinant expression of His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS, BL21(DE3), BL21-CodonPlus(DE3)-RIPL, OverExpress C41(DE3), or OverExpress C43(DE3)pLysS, and recombinant expression of the enzyme in Mycobacterium smegmatis strain mc2 4517, none of these approaches leads to expression of the enzyme in the soluble form, except for strain BL21(DE3)pLysS, recombinant expression of enzyme mutants
gene galEsp2 or galE-2, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene OsUGE-1, phylogenetic analysis of the UGEs from Oryza sativa, recombinant overexpression in Oryza sativa via Agrobacterium tumefaciens-mediated transformation, real-time PCR enzyme expression analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene UGE1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of the enzyme fused to thioredoxin and His6 in Escherichia coli strain BL21(DE3)
gene uge1, is constitutively expressed, recombinant expression in Escherichia coli strain XL-1 blue
gene UGE1, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain
gene UGE2, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain Transetta (DE3)
gene ugeA, DNA and amino acid sequence determination and analysis, cytoplasmic expression of GFP-tagged UgeA in Aspergillus nidulans from a plasmid under control of the wild-type promoter, expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
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genes uge3 and uge5, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3), expression as fluorescence labeled proteins uge3-gfp and uge5-rfp in Aspergillus. fumigatus strain Af293
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mutant enzymes S132A, Y157F, S132A/Y157F and C307Y are expressed in a null-background strain of Saccharomyces cerevisiae. S132a/Y157F and C307Y are also overexpressed in Pichia pastoris
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overexpression in Escherichia coli
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overproduction of MalE-Gne fusion protein in Escherichia coli
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recombinant enzyme overexpression in Thermus thermophilus strain HB27 to an increased capacity of biofilm production, expression of His-tagged enzyme
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recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-Gold (DE3)
recombinant protein is expressed in Escherichia coli
recombinant protein is expressed in Escherichia coli with C-terminal His-tag
To explore the quantitative relationship between GALE activity and galactose metabolism and sensitivity in yeast, a strain is generated in which the expression of GAL10, encoding GALE, was regulated by doxycycline. In brief, a doxycycline-repressible promoter is introduced just upstream of the GAL10 coding sequence in a strain (JFy4763) that was otherwise wild type for all Leloir pathway enzymes and that was engineered to express the appropriate doxycycline-responsive transcriptional activator and repressor protein moieties.
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
Q81JK4, Q81K34
expression in Escherichia coli
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