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EC Tree
The taxonomic range for the selected organisms is: Pisum sativum The enzyme appears in selected viruses and cellular organisms
Synonyms
gal10, udp-galactose 4-epimerase, 4-epimerase, udp-glucose 4-epimerase, udp-galactose-4-epimerase, udp-galactose 4'-epimerase, udp-glucose 4'-epimerase, udp-glucose-4-epimerase, udp-glucose epimerase, gal10p,
more
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UDP-glucose 4-epimerase
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Epimerase, uridine diphosphoglucose
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UDP-D-galactose 4-epimerase
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UDP-galactose 4-epimerase
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UDP-glucose epimerase
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UDPgalactose 4-epimerase
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Uridine diphosphate galactose 4-epimerase
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Uridine diphosphate glucose 4-epimerase
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Uridine diphospho-galactose-4-epimerase
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Uridine diphosphoglucose 4-epimerase
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Uridine diphosphoglucose epimerase
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additional information
PsUGE1 belongs to plant UGE I family
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UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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UDP-alpha-D-glucose
UDP-alpha-D-galactose
UDP-D-glucose
UDP-D-galactose
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r
UDP-D-xylose
UDP-L-arabinose
UDP-galactose
UDP-glucose
UDP-L-arabinose
UDP-D-xylose
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
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r
additional information
?
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UDP-alpha-D-glucose
UDP-alpha-D-galactose
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-
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
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r
UDP-D-xylose
UDP-L-arabinose
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r
UDP-D-xylose
UDP-L-arabinose
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
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r
UDP-galactose
UDP-glucose
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r
UDP-galactose
UDP-glucose
the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
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r
additional information
?
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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
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additional information
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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
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UDP-alpha-D-glucose
UDP-alpha-D-galactose
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r
UDP-D-glucose
UDP-D-galactose
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r
UDP-D-xylose
UDP-L-arabinose
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r
UDP-galactose
UDP-glucose
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r
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additional information
an NAD+ binding motif is GGXGXXG, not required for activity
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additional information
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an NAD+ binding motif is GGXGXXG, not required for activity
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Al3+
enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
Ba2+
enzyme activity is 54.6 U/mg protein at a metal concentration of 1 mM
Ca2+
enzyme activity is 47.8 U/mg protein at a metal concentration of 1 mM
Co2+
enzyme activity is 44.7 U/mg protein at a metal concentration of 1 mM
Cu2+
enzyme activity is 21.8 U/mg protein at a metal concentration of 1 mM
Fe3+
enzyme activity is 20.3 U/mg protein at a metal concentration of 1 mM
Hg2+
1 mM Hg2+ abolishes enzyme function entirely
Li+
enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
Mg2+
enzyme activity is 51.5 U/mg protein at a metal concentration of 1 mM
Mn2+
enzyme activity is 43.2 U/mg protein at a metal concentration of 1 mM
Zn2+
enzyme activity is 17.2 U/mg protein at a metal concentration of 1 mM
additional information
no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
additional information
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no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
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Hg2+
complete inhibition, recombinan t enzyme
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0.29
UDP-D-galactose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.31
UDP-D-glucose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.15
UDP-D-xylose
pH 8.6, 25°C
0.29
UDP-galactose
pH 8.6, 25°C
0.31
UDP-glucose
pH 8.6, 25°C
0.16
UDP-L-arabinose
pH 8.6, 25°C
0.15
UDP-xylose
pH 8.6, 25°C
additional information
additional information
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additional information
additional information
kinetic analysis
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additional information
additional information
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kinetic analysis
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17
UDP-D-xylose
pH 8.6, 25°C
64
UDP-galactose
pH 8.6, 25°C
9
UDP-glucose
pH 8.6, 25°C
23
UDP-L-arabinose
pH 8.6, 25°C
17
UDP-xylose
pH 8.6, 25°C
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115
UDP-D-xylose
pH 8.6, 25°C
220
UDP-galactose
pH 8.6, 25°C
28
UDP-glucose
pH 8.6, 25°C
141
UDP-L-arabinose
pH 8.6, 25°C
115
UDP-xylose
pH 8.6, 25°C
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16.7
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
21.1
purified recombinant detagged enzyme, substrate UDP-L-Ara
49
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
6.67
purified native enzyme, substrate UDP-D-Xyl
6.7
purified native enzyme, substrate UDP-L-Ara
1.7
native protein, substrate is UDP-glucose
1.7
purified native enzyme, substrate UDP-Glc
19.8
native protein, substrate is UDP-galactose
19.8
purified native enzyme, substrate UDP-Gal
38.9
purified recombinant detagged enzyme, substrate UDP-D-Xyl
38.9
specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
4.6
purified recombinant detagged enzyme, substrate UDP-Glc
4.6
recombinant Pisum protein, substrate is UDP-glucose
53.3
purified recombinant detagged enzyme, substrate UDP-Gal
53.3
recombinant Pisum protein, substrate is UDP-galactose
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8.5 - 9
recombinant enzyme
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8.5 - 9
maximum activity of recombinant PsUGE1
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15
recombinant enzyme
15
maximum activity of recombinant PsUGE1
30
native enzyme
30
maximum activity of native enzyme
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UniProt
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gene UGE1
UniProt
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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
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physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
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UGE1_PEA
350
0
38960
Swiss-Prot
Secretory Pathway (Reliability: 3 )
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39000
native Pisum sativum enzyme determined by SDS-PAGE
41000
recombinant enzyme after purification and thrombin digestion
56000
recombinant enzyme after purification on a chelating column
38994
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x * 38994, calculation from nucleotide sequence
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?
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x * 38994, calculation from nucleotide sequence
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40
purified recombinant enzyme, complete inactivation above
40
recombinant Pisum enzyme loses both activities completely at temperatures higher than 40°C
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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
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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
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Lake, M.R.; Williamson, C.L.; Slocum, R.D.
Molecular cloning and characterization of a UDP-glucose-4-epimerase gene (galE) and its expression in pea tissues
Plant Physiol. Biochem.
36
555-562
1998
Pisum sativum
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Kotake, T.; Takata, R.; Verma, R.; Takaba, M.; Yamaguchi, D.; Orita, T.; Kaneko, S.; Matsuoka, K.; Koyama, T.; Reiter, W.D.; Tsumuraya, Y.
Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
Biochem. J.
424
169-177
2009
Pisum sativum (B0M3E8), Pisum sativum, Arabidopsis thaliana (Q42605), Arabidopsis thaliana (Q8LDN8), Arabidopsis thaliana (Q9C7W7), Arabidopsis thaliana (Q9SN58), Arabidopsis thaliana (Q9T0A7)
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