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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
udp-d-xylose 4-epimerase, udp-l-arabinose 4-epimerase,
more
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Epimerase, uridine diphosphoarabinose
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UDP arabinose epimerase
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UDP xylose-4-epimerase 1
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UDP-alpha-D-xylose 4-epimerase
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UDP-arabinose 4-epimerase
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UDP-D-xylose 4-epimerase
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Uridine 5'-diphosphate-D-xylose 4-epimerase
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Uridine diphosphoarabinose epimerase
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UDP-Xyl 4-epimerase
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UDP-xylose 4-epimerase
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Uxe
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UXE1
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UXE2
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UDP-L-arabinose = UDP-D-xylose
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epimerization
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UDP-L-arabinose 4-epimerase
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UDP-alpha-D-xylopyranose
UDP-beta-L-arabinopyranose
UDP-beta-L-arabinopyranose
UDP-alpha-D-xylopyranose
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r
UDP-D-xylopyranose
UDP-beta-L-arabinopyranose
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r
UDP-D-xylose
UDP-L-arabinose
UDP-L-arabinose
UDP-D-xylose
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r
additional information
?
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UDP-alpha-D-xylopyranose
UDP-beta-L-arabinopyranose
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-
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r
UDP-alpha-D-xylopyranose
UDP-beta-L-arabinopyranose
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r
UDP-D-xylose
UDP-L-arabinose
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?
UDP-D-xylose
UDP-L-arabinose
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?
UDP-D-xylose
UDP-L-arabinose
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r
UDP-D-xylose
UDP-L-arabinose
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?
UDP-D-xylose
UDP-L-arabinose
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-
?
UDP-D-xylose
UDP-L-arabinose
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-
r
UDP-D-xylose
UDP-L-arabinose
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?
UDP-D-xylose
UDP-L-arabinose
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r
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?
UDP-D-xylose
UDP-L-arabinose
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?
additional information
?
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity. Changes are correlated with the differences observed in the chemical composition of the cell wall during development
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?
additional information
?
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enzyme UXE, has strict substrate specificity and only catalyzes the interconversion of UDP-D-Xyl and UDP-L-Ara
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?
additional information
?
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enzyme UXE, has strict substrate specificity and only catalyzes the interconversion of UDP-D-Xyl and UDP-L-Ara
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?
additional information
?
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the purified recombinant isoform UXE1 does not catalyze the interconversion of UDP-glucose and UDP-galactose
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?
additional information
?
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the purified recombinant isoform UXE1 does not catalyze the interconversion of UDP-glucose and UDP-galactose
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?
additional information
?
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the purified recombinant isoform UXE1 does not catalyze the interconversion of UDP-glucose and UDP-galactose
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?
additional information
?
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the purified recombinant isoform UXE1 does not catalyze the interconversion of UDP-glucose and UDP-galactose
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?
additional information
?
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity. Changes are correlated with the differences observed in the chemical composition of the cell wall during development
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?
additional information
?
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UDP-galactose, UDP-glucose, UDP-glucuronic acid, UDP-galacturonic acid, UDP-N-acetylglucosamine, and GDP-mannose are no substrates for the enzyme
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?
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UDP-D-xylose
UDP-L-arabinose
UDP-L-arabinose
UDP-D-xylose
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-
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r
additional information
?
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UDP-D-xylose
UDP-L-arabinose
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r
UDP-D-xylose
UDP-L-arabinose
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r
additional information
?
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity. Changes are correlated with the differences observed in the chemical composition of the cell wall during development
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?
additional information
?
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity. Changes are correlated with the differences observed in the chemical composition of the cell wall during development
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?
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NAD+
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NAD+
each molecule of isoform UXE1 contains about one molecule of noncovalently bound NAD+
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Al3+
activity of enzyme towards UDP-xylose is 15.5 U/mg protein at a metal concentration of 1 mM
Ba2+
activity of enzyme towards UDP-xylose is 23.0 U/mg protein at a metal concentration of 1 mM
Ca2+
activity of enzyme towards UDP-xylose is 20.2 U/mg protein at a metal concentration of 1 mM
Co2+
activity of enzyme towards UDP-xylose is 18.6 U/mg protein at a metal concentration of 1 mM
Cu2+
activity of enzyme towards UDP-xylose is 13.9 U/mg protein at a metal concentration of 1 mM
Fe3+
activity of enzyme towards UDP-xylose is 12.1 U/mg protein at a metal concentration of 1 mM
Hg2+
1 mM Hg2+ abolishes enzyme function entirely
Li+
activity of enzyme towards UDP-xylose is 18.1 U/mg protein at a metal concentration of 1 mM
Mg2+
activity of enzyme towards UDP-xylose is 21.3 U/mg protein at a metal concentration of 1 mM
Mn2+
activity of enzyme towards UDP-xylose is 15.5 U/mg protein at a metal concentration of 1 mM
Zn2+
activity of enzyme towards UDP-xylose is 10.2 U/mg protein at a metal concentration of 1 mM
additional information
Mg2+ does not stimulate the activity of the recombinant isoform UXE1. Addition of NADH or NAD+ has no significant effect on activity
additional information
Mg2+ does not stimulate the activity of the recombinant isoform UXE1. Addition of NADH or NAD+ has no significant effect on activity
additional information
Mg2+ does not stimulate the activity of the recombinant isoform UXE1. Addition of NADH or NAD+ has no significant effect on activity
additional information
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Mg2+ does not stimulate the activity of the recombinant isoform UXE1. Addition of NADH or NAD+ has no significant effect on activity
additional information
metal ions are not required for enzyme activity
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p-chloromercuriphenylsulfonate
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inhibition is reversed by Cys
p-hydroxymercuribenzoate
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UDP
15% residual activity at 2 mM
UTP
54% residual activity at 2 mM
additional information
UMP and EDTA do not inhibit the activity of the recombinant isoform UXE1
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additional information
UMP and EDTA do not inhibit the activity of the recombinant isoform UXE1
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additional information
UMP and EDTA do not inhibit the activity of the recombinant isoform UXE1
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additional information
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UMP and EDTA do not inhibit the activity of the recombinant isoform UXE1
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additional information
the enzyme is fully active in the presence of EDTA and is not inhibited by NADH
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dithiothreitol
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dithiothreitol
150% activity at 2 mM
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0.31 - 1.8
UDP-alpha-D-xylopyranose
1.4
UDP-beta-L-arabinopyranose
pH 7.0, at 25°C
0.31
UDP-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
0.016 - 0.5
UDP-L-arabinose
0.31
UDP-alpha-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
1.8
UDP-alpha-D-xylopyranose
pH 7.0, at 25°C
0.015
UDP-D-xylose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.16
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
0.32
UDP-D-xylose
recominant Arabidopsis thaliana enzyme UGE3, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
0.34
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE2, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
0.42
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE4, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
0.43
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE1, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
0.016
UDP-L-arabinose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
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1.5 - 13
UDP-alpha-D-xylopyranose
1.5
UDP-beta-L-arabinopyranose
pH 7.0, at 25°C
13
UDP-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
1.5
UDP-alpha-D-xylopyranose
pH 7.0, at 25°C
13
UDP-alpha-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
0.2
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme
0.4
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme
0.5
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme
13
UDP-D-xylose
recominant Arabidopsis thaliana enzyme UGE3
19
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE1
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0.9 - 42.1
UDP-alpha-D-xylopyranose
1.1
UDP-beta-L-arabinopyranose
pH 7.0, at 25°C
42.1
UDP-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
0.9
UDP-alpha-D-xylopyranose
pH 7.0, at 25°C
42.1
UDP-alpha-D-xylopyranose
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
0.5
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE4, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
1.2
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
3.1
UDP-D-xylose
recominant Arabidopsis thaliana enzyme UGE5, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
40
UDP-D-xylose
recominant Arabidopsis thaliana enzyme UGE3, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
45
UDP-D-xylose
recombinant Arabidopsis thaliana enzyme UGE1, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)
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16.7
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
21.1
recombinant Pisum protein, substrate is UDP-arabinose
22.4
recombinant Pisum protein, substrate is UDP-xylose
38.9
specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
49
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
additional information
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6.7
native protein, substrate is UDP-arabinose
6.7
native protein, substrate is UDP-xylose
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7
assay at
8.6
assay at
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6 - 10
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6: about 30% of maximal activity, 10: about 40% of maximal activity
8.5 - 9
maximum activity of recombinant enzyme
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15
maximum activity of recombinant enzyme
30
assay at
30
maximum activity of native enzyme
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6.93
sequence calculation
9.05
sequence calculation
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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brenda
UXE1; i.e. Albuca bracteata or Ornithogalum longebracteatum
UniProt
brenda
UXE2; i.e. Albuca bracteata or Ornithogalum longebracteatum
UniProt
brenda
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-
brenda
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UniProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
isoform UXE1
UniProt
brenda
isoform UXE2
UniProt
brenda
isoform UXE3
UniProt
brenda
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sterile
brenda
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brenda
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brenda
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brenda
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-
brenda
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brenda
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differentiating and differentiated
brenda
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activity is slightly greater in xylem than in cambium
brenda
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity
brenda
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differentiating and differentiated
brenda
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activity decreases from cambium to xylem
brenda
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity
brenda
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brenda
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following cellulose biosynthesis inhibition, activation of a UDP-D-xylose 4-epimerase gene correlates with increases in arabinose and uronic acid content in seedling cell walls
brenda
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brenda
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brenda
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brenda
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differentiating and differentiated
brenda
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activity is slightly greater in xylem than in cambium
brenda
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differentiating and differentiated
brenda
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity
brenda
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differentiating and differentiated
brenda
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activity decreases from cambium to xylem
brenda
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differentiating and differentiated
brenda
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at the final stage of the differentiation of cambium to xylem there is a decrease in activity
brenda
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a type I membrane protein
brenda
-
brenda
-
brenda
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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
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. Enzyme UXE also plays a key role in carbohydrate partitioning, plant growth and development. UXE is important in the composition of the sugar nucleotide pools
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ARAE1_ARATH
419
0
46311
Swiss-Prot
Mitochondrion (Reliability: 5 )
ARAE1_ORYSJ
421
1
46773
Swiss-Prot
Mitochondrion (Reliability: 5 )
ARAE2_ARATH
417
0
45955
Swiss-Prot
Mitochondrion (Reliability: 5 )
ARAE2_ORYSJ
391
1
42784
Swiss-Prot
other Location (Reliability: 5 )
ARAE3_ARATH
411
0
45155
Swiss-Prot
Mitochondrion (Reliability: 4 )
ARAE3_ORYSJ
406
0
44827
Swiss-Prot
Mitochondrion (Reliability: 5 )
ARAE4_ARATH
436
1
48345
Swiss-Prot
Mitochondrion (Reliability: 3 )
UGE1_ARATH
351
0
39158
Swiss-Prot
other Location (Reliability: 3 )
UGE1_PEA
350
0
38960
Swiss-Prot
Secretory Pathway (Reliability: 3 )
UGE3_ARATH
351
0
38910
Swiss-Prot
other Location (Reliability: 4 )
A0A2P6Q9U4_ROSCH
100
0
10837
TrEMBL
Mitochondrion (Reliability: 2 )
A0A2G9HJY6_9LAMI
417
0
46034
TrEMBL
Mitochondrion (Reliability: 5 )
B9S3M4_RICCO
295
0
32629
TrEMBL
other Location (Reliability: 4 )
A0A2P6Q9Y3_ROSCH
110
0
11803
TrEMBL
Mitochondrion (Reliability: 2 )
A0A2G9HIV0_9LAMI
175
2
19040
TrEMBL
Secretory Pathway (Reliability: 4 )
A0A072VG20_MEDTR
412
1
45480
TrEMBL
Mitochondrion (Reliability: 5 )
A0A2P6Q9W3_ROSCH
107
0
11435
TrEMBL
other Location (Reliability: 3 )
A0A2I0B2D0_9ASPA
54
0
6094
TrEMBL
other Location (Reliability: 3 )
A0A2G9HJI6_9LAMI
206
0
23216
TrEMBL
other Location (Reliability: 2 )
E1SIJ6_PANVC
Pantoea vagans (strain C9-1)
275
0
29476
TrEMBL
-
A0A2I0B8D7_9ASPA
405
1
45131
TrEMBL
Mitochondrion (Reliability: 4 )
A0A5B6YK77_DAVIN
416
2
45803
TrEMBL
Mitochondrion (Reliability: 4 )
G7L9K1_MEDTR
415
1
45977
TrEMBL
Mitochondrion (Reliability: 4 )
B9SV82_RICCO
417
0
45834
TrEMBL
Mitochondrion (Reliability: 3 )
A0A2P6Q6P6_ROSCH
417
1
46031
TrEMBL
Mitochondrion (Reliability: 5 )
C8PNH6_9SPIR
310
0
34564
TrEMBL
-
A0A168GPQ3_ALBBR
416
0
45423
TrEMBL
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A0A168GPR3_ALBBR
418
0
46222
TrEMBL
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Q2LC81_HORVU
405
0
44712
TrEMBL
-
Q2LC82_HORVU
333
0
36636
TrEMBL
-
Q2LC83_HORVU
421
0
46764
TrEMBL
Secretory Pathway (Reliability: 4 )
Q92WA3_RHIME
Rhizobium meliloti (strain 1021)
328
0
35356
TrEMBL
other Location (Reliability: 2 )
UGE4_ARATH
348
0
38123
Swiss-Prot
other Location (Reliability: 2 )
UGE5_ARATH
351
0
38618
Swiss-Prot
-
UGE2_ARATH
350
0
38382
Swiss-Prot
-
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36700
2 * 36700, calculated from amino acid sequence
39000
native Pisum sativum enzyme determined by SDS-PAGE
41000
recombinant enzyme after purification and thrombin digestion
45000
isoform UXE3, calculated from amino acid sequence
47000
isoform UXE1, calculated from amino acid sequence
56000
recombinant enzyme after purification on a chelating column
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homodimer
2 * 36700, calculated from amino acid sequence
?
x * 45400, about, sequence calculation
?
x * 46200, about, sequence calculation
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additional information
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approximately 3% w/w of the protein consists of fatty acids
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additional information
generation of truncated enzyme for expression as soluble protein. The truncated recombinant enzyme is catalytically inactive
additional information
generation of truncated enzyme for expression as soluble protein. The truncated recombinant enzyme is catalytically inactive
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40
recombinant Pisum enzyme loses both activities completely at temperatures higher than 40°C
50
-
1 min, 80% loss of activity
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0-4°C, stable for at least 3 weeks, 50% loss of activity after 2 months
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4°C, purified enzyme, at least 1 week, little or no loss of activity
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Ni-NTA column chromatography
Ni-Sepharose column chromatography
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
purification of the recombinant Arabidopsis enzyme by Ni-NTA affinity chromatography
recombinant His-tagged truncated inactive enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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expressed in Escherichia coli
expression in Agrobacterium tumefaciens
gene UXE1, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain BL21(DE3) by coexpression with chaperones from plasmid pET28atOcUXE1 and chaperone plasmid pGro7, and pET28atOcUXE2 and another chaperone plasmid pKJE7. The recombinant expression in absence of chaperones results in misfolded enzyme in inclusion bodies, expression of full-length His-tagged enzyme is unsuccessful. The truncated recombinant enzyme is catalytically inactive
gene UXE2, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain BL21(DE3) by coexpression with chaperones from plasmid pET28atOcUXE1 and chaperone plasmid pGro7, and pET28atOcUXE2 and another chaperone plasmid pKJE7. The recombinant expression in absence of chaperones results in misfolded enzyme in inclusion bodies, expression of full-length His-tagged enzyme is unsuccessful. The truncated recombinant enzyme is catalytically inactive
isoform UXE1 is expressed in Pichia pastoris
recombinant protein AtUGE1-5 is expressed in Escherichia coli with C-terminal His-tag
recombinant protein is expressed in Escherichia coli
recombinant protein is expressed in Escherichia coli with C-terminal His-tag
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in developing barley endosperm, isoform UXE3 mRNA levels peak at a time when UDP-alpha-D-xylopyranose synthase transcripts also reach a maximum and when arabinoxylan biosynthesis is initiated
in developing barley endosperm, isoforms UXE1 mRNA levels peak at a time when UDP-alpha-D-xylopyranose synthase transcripts also reach a maximum and when arabinoxylan biosynthesis is initiated. Transcript levels for the UXE1 gene are about 4fold higher at 9 days after pollination than in the syncytial and cellularization stages
isoform UXE2 transcript abundance is moderate during the syncytial stage of endosperm development (2-6 days after pollination) but decreases to undetectable levels beyond 6 days after pollination
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Fan, D.F.; Feingold, D.S.
Nucleoside diphosphate-sugar 4-epimerase. II. Uridine diphosphate arabinose 4-epimerase of wheat germ
Plant Physiol.
46
592-595
1970
Triticum aestivum
brenda
Dalessandro, G.; Northcote, D.H.
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Arabidopsis thaliana (O64749), Arabidopsis thaliana (Q9FI17), Arabidopsis thaliana (Q9SA77), Arabidopsis thaliana (Q9SUN3)
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Gu, X.; Lee, S.G.; Bar-Peled, M.
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Zhang, Q.; Shirley, N.J.; Burton, R.A.; Lahnstein, J.; Hrmova, M.; Fincher, G.B.
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