Information on EC 5.1.3.2 - UDP-glucose 4-epimerase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
5.1.3.2
-
RECOMMENDED NAME
GeneOntology No.
UDP-glucose 4-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
show the reaction diagram
; presence of at least one essential Arg at the substrate-binding region of the active site; Ser124 and Tyr149 are likely to play important roles in the catalytic mechanism
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
show the reaction diagram
a nucleoside diphospho-4-ulose of the configuration D-xylo-4-hexosulose is an intermediate in the reaction
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
epimerization
-
of uridine diphosphate (UDP)-glucose to a galactose derivated UDP-galactose
epimerization
-
-
epimerization
-
The reaction mechanism of UGE is thought to occur via transfer of the 4'-OH hydrogen of the sugar to the nicotinamide ring of noncovalently bound NAD+, rotation of the resulting 4'-ketopyranose intermediate in the active site, and transfer of the hydride from the nicotinamide ring of NADH back to C-4 of the sugar.
epimerization
-
-
epimerization
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
epimerization
B0M3E8
-
epimerization
-, Q81JK4, Q81K34
;
epimerization
B1X789
-
epimerization
-
-
specificity for carbon 4, forming a 4-hexosulose intermediate
-
additional information
-, Q58IJ6
catalyses the interconversion of UDP-Gal and UDPGlc; HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
Hordeum vulgare L.
-
catalyses the interconversion of UDP-Gal and UDPGlc; HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
colanic acid building blocks biosynthesis
-
galactose degradation I (Leloir pathway)
-
galactose degradation III
-
Galactose metabolism
-
Metabolic pathways
-
mycolyl-arabinogalactan-peptidoglycan complex biosynthesis
-
stachyose degradation
-
superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis
-
UDP-D-galactose biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-Epimerase
-
-
-
-
6xHis-rGalE
-
-
AtUGE1
Q42605
-
AtUGE2
Q9T0A7
-
AtUGE3
Q8LDN8
-
AtUGE4
Q9C7W7
-
AtUGE5
Q9SN58
-
CaGAL10
-
-
Epimerase, uridine diphosphoglucose
-
-
-
-
Gal10p
-
the first and the last enzyme of the Leloir pathway, galactose mutarotase and UDP-galactose 4-epimerase, are comtained within a single polypeptide chain referred to as Gal10p
Galactowaldenase
-
-
-
-
GalE
B1X789
-
GalE
Q14376
-
GalE
Pyrococcus horikoshii OT-3
O73960
-
-
GNE
Escherichia coli O86:B7
-
-
-
HvUGE1
-, Q58IJ6
-
HvUGE1
Hordeum vulgare L.
-
-
-
HvUGE2
-
-
HvUGE2
Hordeum vulgare L.
-
-
-
HvUGE3
-
-
PsUGE1
B0M3E8
-
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-D-glucose/UDP-D-galactose 4-epimerase
-
-
UDP-Gal 4-epimerase
-, Q58IJ6
-
UDP-Gal 4-epimerase
Hordeum vulgare L.
-
-
-
UDP-galactose 4'-epimerase
-
-
UDP-galactose 4'-epimerase
-
-
UDP-galactose 4'-epimerase
-
-
UDP-galactose 4'-epimerase
-
-
UDP-galactose 4-epimerase
-
-
-
-
UDP-galactose 4-epimerase
-
-
UDP-galactose 4-epimerase
-
-
UDP-galactose 4-epimerase
-
-
UDP-galactose 4-epimerase
-
-
UDP-galactose-4'-epimerase
-
-
UDP-galactose-4'-epimerase
-
-
UDP-galactose-4'-epimerase
-
-
UDP-galactose-4-epimerase
-
-
UDP-galactose-4-epimerase
-
-
UDP-galactose-4-epimerase
B1X789
-
UDP-galactose-4-epimerase
-
-
UDP-galactose-4-epimerase
Q14376
-
UDP-galactose-4-epimerase
A3MUJ4
-
UDP-galactose-4-epimerase
Q9HDU3
-
UDP-Glc 4-epimerase
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
UDP-Glc 4-epimerase
Q81JK4, Q81K34
-
UDP-Glc 4-epimerase
-
-
UDP-Glc 4-epimerase
Homo sapiens CHO-K1
-
-
-
UDP-Glc 4-epimerase
-, Q58IJ6
-
UDP-Glc 4-epimerase
Hordeum vulgare L.
-
-
-
UDP-Glc 4-epimerase
B0M3E8
-
UDP-Glc 4-epimerase
-
-
UDP-GlcNAc 4-epimerase
Q81JK4
-
UDP-GlcNAc/Glc 4-epimerase
-
bifunctional enzyme
UDP-GlcNAc/Glc 4-epimerase
-
-
UDP-GlcNAc/Glc 4-epimerase
Escherichia coli O86:B7
-
-
-
UDP-glucose 4'-epimerase
-
-
UDP-glucose 4-epimerase
-
-
UDP-glucose 4-epimerase
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
UDP-glucose 4-epimerase
Q81JK4, Q81K34
-
UDP-glucose 4-epimerase
-
-
UDP-glucose 4-epimerase
B0M3E8
-
UDP-glucose 4-epimerase
-
-
UDP-glucose epimerase
-
-
-
-
UDP-glucose-4-epimerase
-
-
UDP-glucose/-galactose 4-epimerase
Q9Y7X5
-
UDP-glucose/-galactose 4-epimerase
Schizosaccharomyces pombe ARC039
Q9Y7X5
-
-
UDP-hexose 4-epimerase
-
-
UDP-Xyl 4-epimerase
B0M3E8
-
UDP-xylose 4-epimerase
B0M3E8
-
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
UGE
-, Q58IJ6
-
UGE
Hordeum vulgare L.
-
-
-
UGE1
B0M3E8
-
Uge1p
Schizosaccharomyces pombe ARC039
Q9Y7X5
-
-
Uridine diphosphate galactose 4-epimerase
-
-
-
-
Uridine diphosphate glucose 4-epimerase
-
-
-
-
uridine diphosphate-galactose-4'-epimerase
-
-
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphogalactose-4-epimerase
B1X789
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
additional information
B0M3E8
PsUGE1 belongs to plant UGE I family
CAS REGISTRY NUMBER
COMMENTARY
9032-89-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Columbia-O ecotype
-
-
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
gene BAS5114
UniProt
Manually annotated by BRENDA team
enzyme exists in two distinct forms
-
-
Manually annotated by BRENDA team
NCTC 11168
-
-
Manually annotated by BRENDA team
enzyme exists in two distinct forms
-
-
Manually annotated by BRENDA team
gene ugeA
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
wild type and mutant enzymes K153M and K153A
-
-
Manually annotated by BRENDA team
wild type and mutant enzymes S124A, S124T, and S124V
-
-
Manually annotated by BRENDA team
wild type and mutant enzymes Y149F, S124A, S124V, and S124T
-
-
Manually annotated by BRENDA team
Escherichia coli O86:B7
O86:B7
-
-
Manually annotated by BRENDA team
CHO-K1
-
-
Manually annotated by BRENDA team
Homo sapiens CHO-K1
CHO-K1
-
-
Manually annotated by BRENDA team
Hordeum vulgare L.
L.
-
-
Manually annotated by BRENDA team
Lactobacillus casei CL 87
CL 87
-
-
Manually annotated by BRENDA team
; gene UGE1
UniProt
Manually annotated by BRENDA team
L. cv. Wando
-
-
Manually annotated by BRENDA team
var. pyramidalis
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
UniProt
Manually annotated by BRENDA team
Saccharomyces fragilis
-
-
-
Manually annotated by BRENDA team
gene uge1; strain ARC039, gene uge1
UniProt
Manually annotated by BRENDA team
Schizosaccharomyces pombe ARC039
gene uge1; strain ARC039, gene uge1
UniProt
Manually annotated by BRENDA team
strains YT-1 and NTU103, gene galE
-
-
Manually annotated by BRENDA team
; strains HB8 and HB27, gene galE
-
-
Manually annotated by BRENDA team
Torulopsis candida
-
-
-
Manually annotated by BRENDA team
Trigonella sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
physiological function
-
galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
-
enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis, gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis; galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants; bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
B0M3E8
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
-
GalE plays a key role in lipopolysaccharide biosynthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-D-glucose
?
show the reaction diagram
-
-
-
-
-
CDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
D-fructose
D-tagatose
show the reaction diagram
B1X789
-
-
-
?
D-galactose
D-glucose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-glucose
D-galactose
show the reaction diagram
B1X789
-
-
-
?
D-psicose
D-sorbose
show the reaction diagram
B1X789
-
-
-
?
D-sorbose
D-psicose
show the reaction diagram
B1X789
-
-
-
?
D-tagatose
D-fructose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
-
-
?
TDP-6-deoxy-D-galactose
?
show the reaction diagram
-
-
-
-
-
TDP-D-glucose
TDP-D-galactose
show the reaction diagram
-
-
-
-
TDP-D-glucose
TDP-D-galactose
show the reaction diagram
-
-
-
-
UDP-6-deoxy-D-glucose
?
show the reaction diagram
-
-
-
-
-
UDP-6-deoxygalactose
UDP-6-deoxyglucose
show the reaction diagram
-
-
-
-
UDP-alpha-D-galactose
UDP-alpha-D-glucose
show the reaction diagram
O73960, -
-
-
-
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
show the reaction diagram
Pyrococcus horikoshii OT-3
O73960
-
-
-
?
UDP-D-fucose
?
show the reaction diagram
-
-
-
-
-
UDP-D-galactose-hexodialose
?
show the reaction diagram
-
-
-
-
-
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
-
-
r
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
-
carbohydrate biosynthesis, carbohydrate catabolism
-
-
r
UDP-D-xylose
?
show the reaction diagram
-
-
-
-
-
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
B0M3E8
-, the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
P09147
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Trigonella sp.
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
Torulopsis candida
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
P40801, -
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-, Q58IJ6
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-, Q81JK4, Q81K34
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
A3MUJ4, -
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
B1X789
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
r
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
r
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces fragilis
-
r
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
r
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
-
role of the essential arginine residue in stretching and binding of the substrate
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
enzyme catalyzes the first step of the Lelpoir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
final step of the Leloir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
galactose metabolic pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
glycolysis and TCA cycle, Leloir pathway
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
Q9HDU3
glycolysis and TCA cycle, Leloir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
Leloir pathway of D-galactose catabolism
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
Leloir pathway of galactose metabolism
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
B0M3E8
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
Saccharomyces cerevisiae 106-3D
-
-
-
-
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-
-
-
-
r
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-, Q58IJ6
-
-
-
?
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-
-
-
-
r
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-, Q58IJ6
-
-
-
r
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Hordeum vulgare L.
-
-
-
-
?
UDP-Glc
UDP-Gal
show the reaction diagram
Escherichia coli, Escherichia coli O86:B7
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli O86:B7
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
Q81K34
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
A3MUJ4, -
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
anthocyanin biosynthesis
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
-
-
-
UDP-glucose
UDP-galactose
show the reaction diagram
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
reaction mechanism modelling, overview
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
B0M3E8
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
Homo sapiens CHO-K1
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-L-arabinose
?
show the reaction diagram
-
-
-
-
-
UDP-L-arabinose
UDP-D-xylose
show the reaction diagram
B0M3E8
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
Deoxy-UDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
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
?
-
-
catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism
-
?
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 epimerase shows associated mutarotase activity distinct from the constitutively formed mutarotase activity. Both activities exist in two functionally independent domains
-
?
additional information
?
-
-
UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The epimerase and mutarotase activities are located in different regions of the epimerase holoenzyme
-
?
additional information
?
-
Saccharomyces fragilis
-
enzyme may play a regulatory role in controlling the flux of galactose metabolism
-
-
-
additional information
?
-
P40801, -
xylose-inducible gene
-
-
-
additional information
?
-
-
the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
-
-
-
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
?
-
-
no interconversion of UDP-GalNAc and UDP-GlcNAc
-
-
-
additional information
?
-
-
Leloir pathway of galactose metabolism
-
-
?
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
-
-
-
additional information
?
-
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
-
-
-
additional information
?
-
Q9Y7X5
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
-
additional information
?
-
-, Q81JK4, 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
?
-
Q81K34
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview, no activity with UDP-N-acetylgalactoseamine
-
-
-
additional information
?
-
B0M3E8
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
?
-
Q9Y7X5
Uge1 protein contains only one epimerase domain
-
-
-
additional information
?
-
B1X789
no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
-
-
-
additional information
?
-
Lactobacillus casei CL 87
-
the enzyme plays an essential role in exopolysaccharide formation. Exopolysaccharide synthesis is considerably improved at a controlled pH of 5.0 on galactose as carbon source, and is correlated with higher-induced activities of UDP-glucose pyrophosphorylase and UDP-galactose 4-epimerase under these growth conditions
-
?
additional information
?
-
Schizosaccharomyces pombe ARC039
Q9Y7X5
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview, Uge1 protein contains only one epimerase domain
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
-
-
r
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
-
carbohydrate biosynthesis, carbohydrate catabolism
-
-
r
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-, Q81JK4, Q81K34
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
A3MUJ4, -
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
enzyme catalyzes the first step of the Lelpoir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
final step of the Leloir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
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
show the reaction diagram
-
galactose metabolic pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
glycolysis and TCA cycle, Leloir pathway
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
Q9HDU3
glycolysis and TCA cycle, Leloir pathway
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
Leloir pathway of D-galactose catabolism
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
-
Leloir pathway of galactose metabolism
-
-
r
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
-
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
show the reaction diagram
-
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-Glc
UDP-Gal
show the reaction diagram
Escherichia coli, Escherichia coli O86:B7
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
Escherichia coli, Escherichia coli O86:B7
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
Q81K34
-
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
A3MUJ4, -
-
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
anthocyanin biosynthesis
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
-
-
-
UDP-glucose
UDP-galactose
show the reaction diagram
-
Leloir pathway of membrane polysaccharide synthesis
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
?
UDP-glucose
UDP-galactose
show the reaction diagram
-
the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
-
-
r
UDP-glucose
UDP-galactose
show the reaction diagram
Homo sapiens CHO-K1
-
The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
-
-
r
additional information
?
-
Saccharomyces fragilis
-
enzyme may play a regulatory role in controlling the flux of galactose metabolism
-
-
-
additional information
?
-
P40801, -
xylose-inducible gene
-
-
-
additional information
?
-
-
the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
-
-
-
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
?
-
-
Leloir pathway of galactose metabolism
-
-
?
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
-
-
-
additional information
?
-
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
-
-
-
additional information
?
-
Q9Y7X5
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
-
additional information
?
-
-, Q81JK4, 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
?
-
Q81K34
UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
-
-
-
additional information
?
-
Schizosaccharomyces pombe ARC039
Q9Y7X5
Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
exogenous NAD+ is not required for activity, but removal causes inactivation
NAD+
-
each dimer contains one molecule of NAD+ tightly bound
NAD+
-
absolute requirement for NAD+. Km: 0.27 mM for the liver enzyme, Km: 0.28 mM for the mammary enzyme; Km: 0.29 mM for the thyroid enzyme
NAD+
Torulopsis candida
-
depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+
NAD+
-
contains one molecule of NAD+ per dimer
NAD+
-
NAD+ is very tightly but noncovalently bound in the active site, NAD+ is reduced to NADH in the course of catalysis. NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth
NAD+
-
contains firmly bound NAD+
NAD+
-
not dependent on addition of NAD+
NAD+
-
no requirement for external NAD+
NAD+
-
two nicotinamide cofactors bind in symmetry-related positions in the dimer
NAD+
-
covalently bound
NAD+
-
the amino acid side chains responsible for anchoring the NAD+ to the protein include Asp33, Asn37, Asp66, Tyr157 and Lys161
NAD+
-
coenzyme is tightly bound at the active site. NAD+ functions as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating their dehydrogenation to the common intermediate UDP-4-ketohexopyranoside. NAD+ activation induced by uridine nucleotides is brought about by a conformational change of epimerase that repositions Tyr149 at an increased distance from nicotinamide N1 of NAD+ while maintaining the electrostatic repulsion between Lys153 and nicotinamide N1 of NAD+
NAD+
-
one mol firmly bound per dimer
NAD+
-, Q58IJ6
non-covalently bound, required in bacteria
NAD+
-
1.78 mol of NAD+ per dimer. Each subunit is independently capable of being associated with one molecule of NAD+, suggestive of two NAD+ binding sites of epimerase per dimer
NAD+
-
; is particularly important
NAD+
-
bound to the enzyme via GxxGxxG motif
NAD+
-
; bound to the enzyme via GxxGxxG motif
NAD+
-
one ligand bound per subunit
NAD+
-, Q81JK4, Q81K34
;
additional information
B0M3E8
an NAD+ binding motif is GGXGXXG, not required for activity
-
additional information
Q81K34
contains an NAD+ binding site
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Al3+
B0M3E8
enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
Ba2+
B0M3E8
enzyme activity is 54.6 U/mg protein at a metal concentration of 1 mM
Ca2+
B0M3E8
enzyme activity is 47.8 U/mg protein at a metal concentration of 1 mM
Co2+
B0M3E8
enzyme activity is 44.7 U/mg protein at a metal concentration of 1 mM
Cu2+
B0M3E8
enzyme activity is 21.8 U/mg protein at a metal concentration of 1 mM
Fe3+
B0M3E8
enzyme activity is 20.3 U/mg protein at a metal concentration of 1 mM
Hg2+
B0M3E8
1 mM Hg2+ abolishes enzyme function entirely
Li+
B0M3E8
enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
Mg2+
B0M3E8
enzyme activity is 51.5 U/mg protein at a metal concentration of 1 mM
Mg2+
-, Q81JK4, Q81K34
4 mM are included in assay medium; 4 mM are included in assay medium
Mg2+
Q81K34
-
MgCl2
-
is included in assay medium
Mn2+
B0M3E8
enzyme activity is 43.2 U/mg protein at a metal concentration of 1 mM
NaCl
-
increases the activity
Zn2+
B0M3E8
enzyme activity is 17.2 U/mg protein at a metal concentration of 1 mM
Mn2+
O73960, -
5 mM, activity is increased by 30%
additional information
-
contains none of the common metal ions
additional information
B0M3E8
no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-Cyclohexanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2',3'-O-(2,4,6-Trinitrocyclohexadienylidene)uridine 5'-monophosphate
-
powerful reversible inhibitor
2,3-Butanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2-Hydroxy-5-nitrobenzyl bromide
-
a combination of NAD+ and UDP protects against modification
5'-UMP
-
-
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
Torulopsis candida
-
-
5'-UMP
Saccharomyces fragilis
-
-
5'-UMP
-
strong, competitive
5'-UMP
-
competitive
5'-UMP
-
strong, competitive
5'-UMP
-
epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
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
5,5'-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+
O73960, -
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
-
-
diethyldicarbonate
-
reversal of inhibition by hydroxylamine. Modification of 1 essential histidine residue is responsible for loss in catalytic activity
diethyldicarbonate
-
almost complete inhibition at 5 mM after 30 min incubation
Dimethylsulfoxide
O73960, -
10%, 26% inhibition
fructose 1,6-diphosphate
-
inhibition is enhanced by combination with UMP
galactose 6-phosphate
-
activation of the minor enzyme form
galactose 6-phosphate
-
activation of the minor enzyme form; partial inhibition of major enzyme form
Galactose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
-
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
Escherichia coli, Torulopsis candida
-
-
-
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
-
Hg2+
B0M3E8
complete inhibition, recombinan t enzyme
L-arabinose
-
on treatment with L-arabinose, 2 mM, in presence of UMP, 0.5 mM, both the native enzyme and the reconstituted enzyme are inactivated at an indistinguishable rate of inactivation
L-arabinose
-
epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-arabinose
-
reductive inhibition
L-Arabinose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
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-Xylose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
NaBH4
-
reductive inhibition
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
NADH
-
no inhibition
NADH
-
slightly inhibiting
NADPH
-
very weak inhibitory effect
p-chloromercuribenzoate
-
no inactivation by p-chloromercuribenzoate
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
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
Showdomycin
-
-
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
-
5.0 mM, 25% inhibition
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
UMP
-
5.0 mM, 44% inhibition
Uridine 5'-diphosphate bromoacetol
-
-
Uridine 5'-diphosphate chloroacetol
-
-
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
UTP
-
5.0 mM, 13% inhibition
methanol
O73960, -
10%, 26% inhibition
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
-
additional information
-
inhibited by combination of 100 microM NADH and 10 microM NAD+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
fructose 4-phosphate
-
stimulates
fructose 6-phosphate
-
stimulates
Galactose 1-phosphate
-
stimulates
Galactose 1-phosphate
-
activation of minor enzyme form, no effect on major enzyme form
galactose 6-phosphate
-
activation of minor enzyme form
galactose 6-phosphate
-
activation of minor enzyme form; partial inhibition of major enzyme form
glucose 1-phosphate
-
stimulates
glucose 6-phosphate
-
stimulates
NAD+
-, Q58IJ6
non-covalently bound, released from the enzyme after denaturation with aqueous ethanol. Each enzyme molecule contains one molecule of NAD+
UDP
-
activates the reduction of epimerase-bound NAD+
UMP
-
activates the reduction of epimerase-bound NAD+
glucose 6-phosphate
Saccharomyces fragilis
-
strong activator
additional information
-
does not require external NAD+ for activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
26.4
-
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.23
-
UDP-alpha-D-galactose
O73960, -
pH 6.5, 60C
2.24
-
UDP-alpha-D-glucose
O73960, -
pH 6.5, 60C
0.057
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
B0M3E8
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.31
-
UDP-D-glucose
B0M3E8
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.15
-
UDP-D-xylose
B0M3E8
pH 8.6, 25C
0.04
-
UDP-Gal
-, Q58IJ6
-
0.295
-
UDP-Gal
-
-
0.035
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme L313M
0.04
-
UDP-galactose
-, Q58IJ6
pH 8.0, 25C
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 37C
0.066
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme K257R
0.069
-
UDP-galactose
-
37C, pH 8.8, wild-type enzyme
0.078
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme G319E
0.082
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme N34S
0.089
-
UDP-galactose
-
-
0.093
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme G90E
0.097
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme L183P
0.099
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme R335H
0.1
0.13
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.11
-
UDP-galactose
-
25C, pH 8.8
0.14
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme D103G
0.16
-
UDP-galactose
-
24C, pH 7.0
0.16
-
UDP-galactose
-
37C, 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 24C
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 37C
0.255
-
UDP-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.258
-
UDP-galactose
-
pH 8.9, 50C, recombinant GalE; recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
0.29
-
UDP-galactose
B0M3E8
pH 8.6, 25C
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 24C
0.5
-
UDP-galactose
-
-
0.5
-
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
0.784
-
UDP-galactose
-
37C
0.8
-
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
1
-
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
3.9
-
UDP-galactose
A3MUJ4, -
in 100 mM MES-NaOH (pH 5.5), at 70C
0.16
-
UDP-GalNAc
-, Q58IJ6
; pH 8.0, 25C
0.373
-
UDP-GalNAc
-
-
1.07
-
UDP-GalNAc
-
37C
0.055
-
UDP-Glc
-, Q58IJ6
-
0.37
-
UDP-Glc
-
-
0.2
-
UDP-GlcNAc
-, Q58IJ6
; pH 8.0, 25C
0.323
-
UDP-GlcNAc
-
-
1.087
-
UDP-GlcNAc
-
37C
0.055
-
UDP-glucose
-, Q58IJ6
pH 8.0, 25C
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
B0M3E8
pH 8.6, 25C
0.56
-
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.76
-
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.78
-
UDP-glucose
-
37C
1.2
-
UDP-glucose
-
24C, pH 7.0
0.16
-
UDP-L-arabinose
B0M3E8
pH 8.6, 25C
0.15
-
UDP-xylose
B0M3E8
pH 8.6, 25C
0.0083
-
UDPgalactose
-
mammary enzyme
0.017
-
UDPgalactose
-
liver enzyme
0.026
-
UDPgalactose
-
mutant Y149F
0.048
-
UDPgalactose
-
mutant S124A
0.064
-
UDPgalactose
-
-
0.1
-
UDPgalactose
-
native and renatured enzyme
0.12
-
UDPgalactose
Saccharomyces fragilis
-
-
0.12
-
UDPgalactose
-
-
0.14
-
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
0.16
-
UDPgalactose
-
-
0.18
-
UDPgalactose
-
native and renatured enzyme
0.2
-
UDPgalactose
-
-
0.22
-
UDPgalactose
-
-
0.225
-
UDPgalactose
-
wild type enzyme
0.256
-
UDPgalactose
-
mutant S124T
0.26
-
UDPgalactose
-
-
0.53
-
UDPgalactose
-
-
1.2
-
UDPgalactose
Torulopsis candida
-
-
1.67
-
UDPgalactose
-
-
0.25
-
UDPglucose
-
-
1.4
-
UDPglucose
-
-
2
37
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
additional information
-
additional information
Saccharomyces fragilis
-
enzyme shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate
-
additional information
-
additional information
Saccharomyces fragilis
-
classical hyperbolic kinetics with UDPgalactose, allosteric kinetics with UDPglucose
-
additional information
-
additional information
B0M3E8
kinetic analysis
-
additional information
-
additional information
-
biphasic Michaelis-Menten kinetics, kinetic patterns, overview. Michaelis-Menten relationship of the monomeric epimerase shows hyperbolic dependency
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00026
-
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.00545
-
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
1
-
UDP-alpha-D-galactose
O73960, -
pH 6.5, 60C
1.1
-
UDP-alpha-D-glucose
O73960, -
pH 6.5, 60C
9
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant Arabidopsis thaliana enzyme
20
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant enzyme UGE4
27
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant enzyme UGE3
55
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant Arabidopsis thaliana enzyme UGE2
64
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant enzyme UGE5
17
-
UDP-D-xylose
B0M3E8
pH 8.6, 25C
0.046
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme G90E
0.633
-
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
0.84
-
UDP-galactose
A3MUJ4, -
in 100 mM MES-NaOH (pH 5.5), at 70C
1.1
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme V94M
5
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme D103G
5.1
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme K257R
5.8
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme L313M
11
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme L183P
12.9
-
UDP-galactose
-
-
15
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme R335H
21
-
UDP-galactose
-, Q58IJ6
25C, 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
-
37C, pH 8.8, mutant enzyme G319E
32
-
UDP-galactose
-
37C, pH 8.8, mutant enzyme N34S
36
-
UDP-galactose
-
37C, 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 25C
55.32
-
UDP-galactose
-
pH 8.9, 50C, recombinant GalE
64
-
UDP-galactose
B0M3E8
pH 8.6, 25C
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 25C
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
-
37C
500
-
UDP-galactose
-
24C, pH 7.0
750
-
UDP-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.12
-
UDP-GalNAc
-, Q58IJ6
25C, pH 8.0
247.9
-
UDP-GalNAc
-
37C
0.07
-
UDP-GlcNAc
-, Q58IJ6
25C, pH 8.0
82.3
-
UDP-GlcNAc
-
37C
2
8
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
9
-
UDP-glucose
B0M3E8
pH 8.6, 25C
11
-
UDP-glucose
-, Q58IJ6
25C, pH 8.0
18
-
UDP-glucose
-
24C, 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).
73.95
-
UDP-glucose
-
37C
23
-
UDP-L-arabinose
B0M3E8
pH 8.6, 25C
17
-
UDP-xylose
B0M3E8
pH 8.6, 25C
0.073
-
UDPgalactose
-
mutant Y149F
0.265
-
UDPgalactose
-
,mutant S124A
64.8
-
UDPgalactose
-
-
248
-
UDPgalactose
-
mutant S124T
500
-
UDPgalactose
-
-
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
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.7e-06
-
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
9162
2.3e-05
-
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
9372
4.34
-
UDP-alpha-D-galactose
O73960, -
pH 6.5, 60C
87891
0.49
-
UDP-alpha-D-glucose
O73960, -
pH 6.5, 60C
219166
103
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
17630
350
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
17630
397
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
17630
435
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
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
17630
578
-
UDP-D-galactose
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
17630
115
-
UDP-D-xylose
B0M3E8
pH 8.6, 25C
17636
0.78
-
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
17639
0.79
-
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
17639
46
-
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
17639
214.4
-
UDP-galactose
-
pH 8.9, 50C, recombinant GalE
17639
220
-
UDP-galactose
B0M3E8
pH 8.6, 25C
17639
232
-
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25C
17639
3333
-
UDP-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
17639
28
-
UDP-glucose
B0M3E8
pH 8.6, 25C
17641
141
-
UDP-L-arabinose
B0M3E8
pH 8.6, 25C
17642
115
-
UDP-xylose
B0M3E8
pH 8.6, 25C
137491
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
5'-UMP
-
25C, pH 8.8
0.036
-
UDP
-, Q58IJ6
; 25C, pH 8.0
0.032
-
UMP
-, Q58IJ6
; 25C, pH 8.0
0.2
-
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
pH 8.8
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14
-
bisprasin
-
-
5.6
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
-
-
12
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
-
-
17
-
Diethylstilbestrol
-
-
75
-
Diethylstilbestrol
-
-
0.014
-
ebselen
-
-
0.62
-
ebselen
-
-
3.1
-
Ethacrynic acid
-
-
14
-
Ethacrynic acid
-
-
0.5
-
haloprogin
-
-
13
-
haloprogin
-
-
3.6
-
psammaplin A
-
-
15
-
psammaplin A
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.6
-
-
GALE activity evaluated in samples by monitoring the conversion of UDP-gal to UDP-glc. Assays stopped by the addition of 237.5 microliter of ice-cold water followed immediately by filtration through 0.2-micrometer nylon micro-spin columns (Corning) to remove proteins and particulates before high performance liquid chromatography analysis.
1.7
-
B0M3E8
native protein, substrate is UDP-glucose; purified native enzyme, substrate UDP-Glc
4.6
-
B0M3E8
purified recombinant detagged enzyme, substrate UDP-Glc; recombinant Pisum protein, substrate is UDP-glucose
6.67
-
B0M3E8
purified native enzyme, substrate UDP-D-Xyl
6.7
-
B0M3E8
purified native enzyme, substrate UDP-L-Ara
7.9
-
-
-
16.7
-
B0M3E8
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
19.8
-
B0M3E8
native protein, substrate is UDP-galactose; purified native enzyme, substrate UDP-Gal
21.1
-
B0M3E8
purified recombinant detagged enzyme, substrate UDP-L-Ara
38.9
-
B0M3E8
purified recombinant detagged enzyme, substrate UDP-D-Xyl; specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
49
-
B0M3E8
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
53.3
-
B0M3E8
purified recombinant detagged enzyme, substrate UDP-Gal; recombinant Pisum protein, substrate is UDP-galactose
66
-
-
liver
210
-
-
mammary
216.7
-
-
-
233.3
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.3
-
activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3
5.5
-
A3MUJ4, -
-
6.5
-
O73960, -
-
7.5
-
B1X789
-
8
9.5
-, Q58IJ6
; interconversion of UDP-glucose and UDP-galactose
8
-
-, Q81JK4, Q81K34
assay at; assay at
8
-
Q81K34
assay at
8.5
9
B0M3E8
recombinant enzyme
8.5
-
Trigonella sp.
-
-
8.6
-
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
assay at; assay at; assay at; assay at; assay at
8.6
-
B0M3E8
assay at
8.7
-
Q9Y7X5
assay at
8.9
-
-
assay at
9
-
-
; recombinant enzyme
9.5
-
-
-
9.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7
-
MES buffer
6
10.5
-
about 65% of maximal activity at pH 6 and 10.5
6
9
O73960, -
pH 6.0: about 80% of maximal activit, pH 9.0: about 50% of maximal activity
6.4
9.6
-
6.4: 68% loss of maximal activity, 9.6: 79% of maximal activity
6.5
9.5
-
Tris/HCl buffer
6.6
9.2
-
about 50% of maximal activity at pH 6.6 and 9.2
6.7
8.1
-
6.7: 91% of maximal activity, 8.1: 88% of maximal activity
7
9.7
-
7: about 50% of maximal activity, 9.7: about 40% of maximal activity
7.6
9.5
-
7.6: about 25% of maximal activity, 9.5: maximal activity
8.5
9
B0M3E8
maximum activity of recombinant PsUGE1
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
B0M3E8
maximum activity of recombinant PsUGE1; recombinant enzyme
30
-
B0M3E8
maximum activity of native enzyme; native enzyme
30
-
Q9Y7X5
assay at
35
-
B1X789
-
37
-
-
assay at
37
-
-, Q81JK4, Q81K34
assay at; assay at
37
-
Q81K34
assay at
50
-
-
; recombinant enzyme
65
-
O73960, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q58IJ6
levels of HvUGE1 mRNA are low in day 1 and day 3 coleoptiles, increases approximately 28fold in day 5 coleoptiles
Manually annotated by BRENDA team
-
from adults and newborn infants
Manually annotated by BRENDA team
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
Manually annotated by BRENDA team
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
Manually annotated by BRENDA team
-, Q58IJ6
expression of HvUGE1 is highest in leaf tips, rapidly decreases to very low levels in the basal region of the leaves
Manually annotated by BRENDA team
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
Manually annotated by BRENDA team
-, Q58IJ6
mRNA levels of HvUGE1 are very high in the maturation zone compared with other regions of the root
Manually annotated by BRENDA team
-
Heterodera schachtii parasitism strongly downregulates RDH1 expression in the root 3 days after inoculation
Manually annotated by BRENDA team
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
Manually annotated by BRENDA team
Trigonella sp.
-
-
Manually annotated by BRENDA team
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
Manually annotated by BRENDA team
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
Manually annotated by BRENDA team
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
Manually annotated by BRENDA team
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
-
Manually annotated by BRENDA team
B0M3E8
; the bifunctional UDP-Glc 4-epimerase/UDP-Xyl 4-epimerase, encoded by UGE1, in the cytosol is distinct from the UDP-Xyl 4-epimerase in the Golgi apparatus
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
-
determined by SDS-PAGE and MALDI-TOF mass spectrometry
36900
-
-, Q81JK4, Q81K34
predicted by amino acid sequence
37000
-
-
MALDI-TOF MS
37000
-
-
by sequence analyses
37800
-
-, Q81JK4, Q81K34
predicted by amino acid sequence
38270
-
-
MALDI-TOF MS
38800
-
-
gel filtration
39000
-
-, Q58IJ6
each subunit
39000
-
B0M3E8
native Pisum sativum enzyme determined by SDS-PAGE
40000
-
-
mammary and liver enzyme, gel filtration
40000
-
-
gel filtration
40200
-
-
gel filtration
40300
-
-
gel filtration
40800
-
-
gel filtration
41000
-
B0M3E8
recombinant enzyme after purification and thrombin digestion
41100
-
-
gel filtration
42000
-
-
nickel affinity chromatography
51000
-
A3MUJ4, -
gel filtration
56000
-
B0M3E8
recombinant enzyme after purification on a chelating column
70000
-
Trigonella sp.
-
gel filtration
70000
-
O73960, -
gel filtration
75480
-
-
-
76000
-
-
sucrose density gradient centrifugation
78000
-
-
gel filtration
79000
-
-
equilibrium centrifugation
79000
-
-
native and renatured enzyme, gel filtration
80000
-
-
sedimentation equilibrium studies
80000
-
-
gel filtration
83000
-
-
gel filtration
84000
-
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
90000
-
-
gel filtration
91000
-
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
98000
-
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
103000
-
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
120000
-
-
gel filtration
120000
-
-
sedimentation equilibrium measurement, addition of NAD+, active dimeric enzyme form
158000
-
-
gel filtration
160000
-
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, dimeric form, gel filtration
183000
187000
-
sucrose density gradient centrifugation, gel filtration
240000
-
-
sedimentation equilibrium measurement, addition of NAD+, 0.01 M Tris buffer with cations, active tetrameric form
320000
-
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, tetrameric form, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38266, calculation from nucleotide sequence
?
-
x * 37000, calculation from nucleotide sequence
?
-
x * 35400, calculation from nucleotide sequence
?
-
x * 40000, SDS-PAGE
?
-
x * 38994, calculation from nucleotide sequence
?
-, Q58IJ6
x * 39000, recombinant enzyme, SDS-PAGE
?
-
x * 40600, recombinant plasmid-expressed UgeA, SDS-PAGE
dimer
-
2 * 59000, SDS-PAGE
dimer
-
2 * 78000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 60000, enzyme exists in an active dimeric and an active tetrameric form
dimer
-
2 * 38000, 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 * 42000, SDS-PAGE
dimer
-
2 * 39000
dimer
-
2 * 75000
dimer
-
2 * 75000, SDS-PAGE
dimer
-, Q58IJ6
homodimer, 2 * 39000
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
-
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.
dimer
-
2 * 38800, gel filtration
dimer
Escherichia coli O86:B7
-
2 * 38800, gel filtration
-
dimer
Hordeum vulgare L.
-
homodimer, 2 * 39000
-
dimer
Saccharomyces cerevisiae 106-3D
-
2 * 78000, SDS-PAGE
-
homodimer
-
a homodimer, containing one catalytic site and one NAD+ as cofactor per subunit, not showing fast association-dissociation
homodimer
A3MUJ4, -
2 * 32000, SDS-PAGE
homodimer
O73960, -
2 * 35000, SDS-PAGE
homodimer
Pyrococcus horikoshii OT-3
-
2 * 35000, SDS-PAGE
-
monomer
-
2 * 36700, SDS-PAGE; 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 * 60000, enzyme exists in an active dimeric and an active tetrameric form
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
additional information
P40801, -
nucleotide sequence
additional information
-
nucleotide sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of the oxidized and reduced forms of UDP-galactose 4-epimerase
-
crystal structure of the ternary complex of UDP-galactose 4-epimerase with NADH and UDP-phenol
-
crystallization of the epimerase/UDP-GLcNAc/NADH abortive complex
-
suitable crystallization conditions are both at room temperature and at 4C using sparse matrix screen and the hanging drop method of vapor diffusion. The best crystals are observed growing from polyethylene glycol 8000 and potassium chloride and in the presence of 2 mM NAD+. Typical large crystals are ontained from 18-20% polyethylene glycol 8000, 100 mM Hepes, pH 7.5, and 250 mM KCl at room temperature, crystallization of a epimerase/NADH/UDP-glucose ternary complex
-
sitting drop vapor diffusion method, using 29% (v/v) 2-ethoxyethanol and 0.1 M cacodylate buffer (pH 6.6), at 20C
A3MUJ4, -
hanging drop vapor diffusion methodthree-dimensional structure of gal10p in complex with NAD+, UDP-glucose, and beta-D-galactose is determined to 1.85 A resolution. Space group I222 with unit cell dimensions of a = 120.9 A, b = 125.2 A and c = 142.3 A. The asymmetric unit contains one monomer
-
hanging drop method
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
O73960, -
highly stable
5.5
10
-
stable, monomeric and dimeric form
7
-
-
unstable below
7
-
Trigonella sp.
-
unstable below
8.5
-
-
25C, 24 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
pH 7.0, 4 h stable, native enzyme
24
-
-
2 h, stable in presence of 1% bovine serum albumin, 0.5 mM dithiothreitol or 1 mM mercaptoethanol
25
-
-
60 min, 26% loss of activity
25
-
-
pH 8.5, 24 h, stable
30
-
-
53% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
30
-
-
53% loss of activity within 10 min, partial protection by NAD+, up to a concentration of 7 mM
37
-
-
85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
37
-
-
85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM. Partial protection by addition of NAD+ up to a concentration of 1 mM
40
-
B0M3E8
purified recombinant enzyme, complete inactivation above; recombinant Pisum enzyme loses both activities completely at temperatures higher than 40C
41
-
Saccharomyces fragilis
-
2 min, desensitization by heat converts the enzyme to its ultimate catalytic form
42
-
Saccharomyces fragilis
-
7 min, inactivation by dissociation of NAD+
45
-
Saccharomyces fragilis
-
3 min, inactivation by dissociation of NAD+
46
-
-
no inactivation after several h
47
-
-
the melting temperature of the recombinant enzyme is at 47C
50
-
-
inactivation above, monomeric and dimeric form
50
-
-
wild-type enzyme loses 20% of its activity after 8 min, mutant enzyme S124A/Y149F loses 80% of its activity after 8 min
60
-
O73960, -
1 h, stable up to
80
-
-
purified recombinant enzyme, 30 min, loss of 78% activity; treatment at 80C for 30 min reduces the enzyme activity by 78%
90
-
-
enzyme is stable at 90C, after incubating at this temperature for 10 min, 90% of the enzymatic activity remains; purified recombinant enzyme, 10 min, loss of 10% activity
100
-
Q81K34
5 min, purified recombinant enzyme, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol is required for stability to freezing and thawing
-
unstable in absence of mercaptoethanol or dithiothreitol
-
uridine nucleotides provide almost total protection against the apparent first order inactivation of epimerase by trypsin. NAD+ partially protects against trypsin inactivation
-
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
-
when trypsinized in the presence of 2.5 mM 5'-UMP, the mutarotase activity is lost in a time-dependent manner without affecting the epimerase activity. Proteolysis under identical conditions in the presence of 6.7 mM galactose or fructose leads to reversal of this protection - epimerase activity is completely lost whereas mutarotase activity is 90% protected
-
more than 80% loss of activity after freeze drying
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diethyldicarbonate
-
incubation of the recombinant His6-tagged protein with increasing concentrations of diethyldicarbonate (1.0-5.0 mM) results in a time-dependent loss of activity
Glycerol
-
the use of glycerol as a cosolvent enhances the GalE thermostability significantly. The enzyme in 50% glycerol can retain 90% of its activity, whereas only 20% activity is observed for the identically treated control enzyme
urea
-
denaturation by 8 M urea at pH 7.0 causes 85% loss of ist secondary structure and dissociation of its constituent molecules
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C or -20C, 0.2 mg/ml enzyme concentration, 0.01 M potassium phosphate buffer, pH 7.5. About 60% of the initial activity remains for 3 months at 4C without any protector, and in the presence of 20% glycerol more than 80% of the activity remains
-
-20C, dilute solutions of highly purified liver or mammary enzyme are very stable in the presence of 20 to 200 mM potassium phosphate, 20% glycerol, 1 mM mercaptoethanol, at pH 7.6, 10% loss of activity after 6 months
-
4C, dilute solutions of highly purified liver or mammary enzyme are very stable in the presence of 20 to 200 mM potassium phosphate, 20% glycerol, 1 mM mercaptoethanol, at pH 7.6
-
-20C, 50% glycerol, stable for 6 months
-
stable for several months if mixed with an equal volume of glycerol and stored in liquid nitrogen
-
-20C, pH 8, stable in presence of glycerol for 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sepharose anion exchange chromatography; Ni2+-NTA affinity chromatography
-
purification of the recombinant Arabidopsis enzyme by Ni-NTA affinity chromatography; purification of the recombinant Arabidopsis enzyme by Ni-NTA affinity chromatography; purification of the recombinant enzyme by Ni-NTA affinity chromatography; purification of the recombinant enzyme by Ni-NTA affinity chromatography; purification of the recombinant enzyme by Ni-NTA affinity chromatography
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration; by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration
-, Q81JK4, Q81K34
recombinant enzyme from Escherichia coli strain BL21(DE3)
Q81K34
MalE-Gne fusion protein overproduced in Escherichia coli
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
Ni+ affinity column chromatography
B1X789
recombinant enzyme
-
nickel agarose column chromatography
-
recombinant enzyme
-
recombinant wild-type and mutant enzymes S132A, Y157F, S132A/Y157F and C307Y
-
purification of the native enzyme from pea sprouts by ion exchange chromatography and gel filtration, further purification on a hydroxyapatite column, purification of recombinant enzymes by ion exchange chromatography; recombinant fusion enzyme 2.33fold from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, native UGE1 334fold from sprouts by ammonium sulfate fractionation and a chromatographic procedure
B0M3E8
DEAE-Toyopearl column chromatography and Superdex 200 gel filtration
A3MUJ4, -
recombinant enzyme
-
recombinant His-tagged enzyme by nickel affinity chromatography
-
by using nickel-NTA affinity chromatography; recombinant His-tagged enzyme by nickel affinity chromatography
-
partial
Trigonella sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
expression in Escherichia coli
-
expression in Escherichia coli and Saccharomyces cerevisiae
-
recombinant protein is expressed in Escherichia coli with C-terminal His-tag; recombinant protein is expressed in Escherichia coli with C-terminal His-tag; recombinant protein is expressed in Escherichia coli with C-terminal His-tag; recombinant protein is expressed in Escherichia coli with C-terminal His-tag; recombinant protein is expressed in Escherichia coli with C-terminal His-tag
Q42605, Q8LDN8, Q9C7W7, Q9SN58, Q9T0A7
expression in Escherichia coli; expression in Escherichia coli
-, Q81JK4, Q81K34
gene BAS5114, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
Q81K34
expression in Sinorhizobium meliloti
-
overproduction of MalE-Gne fusion protein in Escherichia coli
-
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
-
expressed in Escherichia coli ER2566 cells
B1X789
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 Saccharomyces cerevisiae EBY100.
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
expressed in Escherichia coli Rosetta cells and in a gal10-null strain of Saccharomyces cerevisiae strain JFy3835
-
expression in Escherichia coli
-
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 Pichia pastoris
-
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
-
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
-
expression in Escherichia coli
-, Q58IJ6
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); recombinant protein is expressed in Escherichia coli
B0M3E8
expressed in Escherichia coli BL21(DE3) cells
A3MUJ4, -
expression in Escherichia coli
O73960, -
expression in Escherichia coli
-
overexpression in Escherichia coli
-
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.
-
gene uge1, is constitutively expressed, recombinant expression in Escherichia coli strain XL-1 blue
Q9Y7X5
expression of His-tagged enzyme
-
expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein; recombinant enzyme overexpression in Thermus thermophilus strain HB27 to an increased capacity of biofilm production, expression of His-tagged enzyme
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
uge1 is not induced by glucose
Q9Y7X5
uge1 is not induced by glucose
Schizosaccharomyces pombe ARC039
-
-
overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K153N
-
the mutation affects the catalytic activity only slightly, however, the NAD+ binding potential is reduced dramatically
Y149G
-
the mutant is completely inactive
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
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
N179S
B1X789
the 4-epimerization of tagatose is enhanced 2fold in this mutant
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
-
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/Y149F
-
mutation causes a 13C downfield perturbation of 2.8 ppm to 152.7 ppm
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 50C compared to 20% inactivation of the wild-type enzyme
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
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.
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
-
mutation results in a 13C downfield perturbation of 2.7 ppm to 152.6 ppm
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
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
S306Y
Escherichia coli O86:B7
-
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
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
D69E
-
the mutant shows reduced activity compared to the wild-type enzyme
E165K
-
unstable mutant
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
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
K257R
-
the ratio of turnover number to Km-value is 6.7fold lower than the wild-type ratio
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
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
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
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
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
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
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
W336X
-
unstable mutant
Y105C
-
the mutant demonstrates 13% residual activity
Y149G/K153N
-
the mutant is completely inactive
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
Y157F
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
additional information
A3MUJ4, -
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
Q9Y7X5
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
Schizosaccharomyces pombe ARC039
-
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
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
denatured by 8 M urea at pH 7.0 to a state having 15% of residual secondary structure. Dilution of the denaturant by 20 mM potassium phosphate, pH 8.5, leads to functional reconstitution of the enzyme. Reactivation follows a socond-order kinetics
-
dilution of the denaturant urea by buffer at pH 8.5 leads to functional reconstitution of the dimeric holoenzyme. The refolding process is biphasic: after 2 min an equilibrium conformer is formed having 72% of its native secondary structure and by 60 min reactivation becomes complete. The early intermediate has lower energy of activation against thermal denaturation than the reactivated state
-
purified enzyme dimer consists of a mixture of catalytically active subunits designated enzyme-NAD+ and inactive, abortive complexes designated enzyme-NADH-uridine nucleotide, in which the uridine nucleotide may be UDPglucose, UDPgalactose, or UDP. The abortive complexes are transformed into active enzyme-NAD+ by denaturation of the purified enzyme at 4C in 6 M guanidine hydrochloride buffered at pH 7.0 in the presence of 0.126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 mM for 2 h. The renatured enzyme is fully active and contains negligible amounts of NADH and uridine nucleotides
-
denaturation in presence of 8 M urea. Dilution of the denaturant by sodium phosphate buffer, 20 mM, pH 7.0, containing 1 mM NAD+ recovers the activity to the extent of 80-100%
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
drug design
medicine
-
The absence of CaGAL10 alone does not significantly reduce virulence in mouse model studies, but since it leads to increased drug sensitivity, it can be explored as a potential drug target in combination with other candidacidal drugs. Thus the UDP-galactose-4-epimerase plays an important role in the biology of the human pathogen, Candida albicans, like in the case of several other pathogens.
synthesis
-
preparation of a fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, shows kinetic advantages in that the initial velocity to produce glucose 1-phosphate from UDPgalactose an
medicine
-
Trypanosoma brucei GalE is a validated drug target for African sleeping sickness. The Trypanosoma brucei enzyme can be selectively inhibited by small molecules that are not substrate analogues in vitro, although the mechanism of cytotoxicity of these inhibitors is unconfirmed. Of the compounds screened, ethacrynic acid displays the best therapeutic index, but is clinically used as a loop diuretic and was found to form multiple covalent adducts with TbGalE in vitro, limiting its potential as a lead compound.
medicine
-
Galactosylation of one or more glycoprotein(s), most likely in the endosomal/lysosomal system, is essential for the survival of bloodstream form Trypanosoma brucei. GalE-encoded epimerase and the downstream UDP-Gal transporters and UDP-Gal-dependent glycosyltransferases may be exploitable as drug targets.