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Information on EC 5.1.3.6 - UDP-glucuronate 4-epimerase for references in articles please use BRENDA:EC5.1.3.6Word Map on EC 5.1.3.6
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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UDP-glucuronate 4-epimerase
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UDP-glucuronate = UDP-D-galacturonate
UDP-glucuronate = UDP-D-galacturonate
formation of a 4-keto intermediate
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UDP-glucuronate = UDP-D-galacturonate
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epimerization
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epimerization
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specific for C-4 of the glycuronosyl moiety
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L-ascorbate biosynthesis V
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UDP-alpha-D-galacturonate biosynthesis I (from UDP-D-glucuronate)
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Amino sugar and nucleotide sugar metabolism
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UDP-glucuronate 4-epimerase
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Epimerase, uridine diphosphoglucuronate
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UDP glucuronic epimerase
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UDP-D-galacturonic acid 4-epimerase
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UDP-D-glucuronate-4-epimerase
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UDP-D-glucuronic acid 4-epimerase
UDP-galacturonate 4-epimerase
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UDP-glucuronic acid 4-epimerase
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uridine diphosphate galacturonate 4-epimerase
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Uridine diphospho-D-galacturonic acid 4-epimerase
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Uridine diphosphoglucuronate epimerase
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Uridine diphosphoglucuronic epimerase
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AtUGlcAE1
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GAE
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GAE1
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GAE2
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GAE3
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GAE4
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GAE6
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isoform
UDP-D-glucuronic acid 4-epimerase
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UDP-D-glucuronic acid 4-epimerase
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UDP-GlcA 4-epimerase
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UDP-GlcA 4-epimerase3
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brenda
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cultivar Xuzhou 142
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UniProt
brenda
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brenda
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type 1
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UniProt
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SwissProt
brenda
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SwissProt
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SwissProt
brenda
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SwissProt
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-
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-
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cv. Columbia-0
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-
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cv. Columbia-0
SwissProt
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syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
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physiological function
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GAE is necessary for Arabidopsis root hair growth
physiological function
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GAE delivers the main substrate for pectin biosynthesis
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UDP-D-glucuronate
UDP-D-galacturonate
UDP-glucuronate
UDP-D-galacturonate
UDPglucuronate
UDP-D-galacturonate
additional information
?
-
UDP-D-glucuronate
UDP-D-galacturonate
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-
-
-
?
UDP-D-glucuronate
UDP-D-galacturonate
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recombinant AtUGlcAE1DELTA1-64 favors the formation of UDP-D-galacturonate over UDP-glucuronate
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r
UDP-D-glucuronate
UDP-D-galacturonate
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-
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-
?
UDP-D-glucuronate
UDP-D-galacturonate
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-
-
?
UDP-D-glucuronate
UDP-D-galacturonate
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equilibrium constant in direction of UDP-galacturonate formation is 1.3
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r
UDP-glucuronate
UDP-D-galacturonate
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r
UDP-glucuronate
UDP-D-galacturonate
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-
-
?
UDP-glucuronate
UDP-D-galacturonate
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-
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r
UDP-glucuronate
UDP-D-galacturonate
the recombinant enzyme establishes a 1.3:1 equilibrium between UDP-D-galacturonate and UDP-glucuronate
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r
UDP-glucuronate
UDP-D-galacturonate
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r
UDP-glucuronate
UDP-D-galacturonate
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r
UDPglucuronate
UDP-D-galacturonate
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-
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UDPglucuronate
UDP-D-galacturonate
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UDPglucuronate
UDP-D-galacturonate
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UDPglucuronate
UDP-D-galacturonate
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UDPglucuronate
UDP-D-galacturonate
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UDPglucuronate
UDP-D-galacturonate
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UDPglucuronate
UDP-D-galacturonate
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additional information
?
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enzyme is required for the nucleoside diphosphate sugar interconversion
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additional information
?
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no epimerization of UDP-D-glucose and UDP-D-xylulose
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additional information
?
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no epimerization of UDP-D-glucose and UDP-D-xylulose
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additional information
?
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no epimerization of UDP-D-glucose and UDP-D-xylulose
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additional information
?
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no epimerization of UDP-D-glucose and UDP-D-xylulose
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additional information
?
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enzyme is required for the nucleoside diphosphate sugar interconversion
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additional information
?
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the enzyme is required for capsular biosynthesis
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?
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UDP-glucuronate
UDP-D-galacturonate
additional information
?
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UDP-glucuronate
UDP-D-galacturonate
Q9LIS3
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r
UDP-glucuronate
UDP-D-galacturonate
Q6K9M5
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r
UDP-glucuronate
UDP-D-galacturonate
Q304Y2
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r
additional information
?
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enzyme is required for the nucleoside diphosphate sugar interconversion
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additional information
?
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enzyme is required for the nucleoside diphosphate sugar interconversion
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additional information
?
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the enzyme is required for capsular biosynthesis
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?
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NADP+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
NAD+
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50 nM to 5 mM, does not affect activity
NAD+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
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ADP-Ara
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2 mM, about 55% inhibition
KCl
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above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
p-hydroxymercuribenzoate
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reactivation by NAD+ and 2-mercaptoethanol
UDP-Xyl
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2 mM, about 60% inhibition
GMP
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NaCl
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above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
NaCl
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progressive decrease in activity above 100 mM NaCl, activity drops below 50% at 250 mM
UDP
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2 mM, about 60% inhibition
UDP
2 mM, strong inhibition of recombinant ZmUGlcAE1-47
UDP-xylose
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UDP-xylose
2 mM, strong inhibition of recombinant ZmUGlcAE1-47
UMP
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additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
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additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
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0.23 - 0.72
UDP-D-glucuronate
0.19 - 0.426
UDP-glucuronate
0.23
UDP-D-glucuronate
25°C, pH 7.9, recombinant enzyme
0.24
UDP-D-glucuronate
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pH 7.5, 37°C
0.72
UDP-D-glucuronate
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0.19
UDP-glucuronate
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0.259
UDP-glucuronate
recombinant OsUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
0.358
UDP-glucuronate
recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6
0.397
UDP-glucuronate
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, in 0.1 M sodium phosphate, pH 7.6
0.426
UDP-glucuronate
recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
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0.9 - 37.4
UDP-glucuronate
0.9
UDP-glucuronate
recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6
10
UDP-glucuronate
recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
10.1
UDP-glucuronate
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, in 0.1 M sodium phosphate, pH 7.6
37.4
UDP-glucuronate
recombinant OsUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
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0.0731 - 0.3051
UDP-xylose
0.0632
UDP
recombinant ZmUGlcAE, position 1-47 is lacking
0.1107
UDP
recombinant AtUGlcAE3, position 1-53 is lacking
0.1145
UDP
recombinant OsUGlcAE3, position 1-53 is lacking
0.1341
UDP
recombinant AtUGlcAE2, position 1-68 is lacking
0.1436
UDP
recombinant AtUGlcAE1, position 1-64 is lacking
0.0731
UDP-xylose
recombinant ZmUGlcAE, position 1-47 is lacking
0.1599
UDP-xylose
recombinant OsUGlcAE3, position 1-53 is lacking
0.2473
UDP-xylose
recombinant AtUGlcAE3, position 1-53 is lacking
0.2972
UDP-xylose
recombinant AtUGlcAE1, position 1-64 is lacking
0.3051
UDP-xylose
recombinant AtUGlcAE2, position 1-68 is lacking
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7.2 - 7.8
optimal pH in phosphate buffer for the activity of recombinant enzyme ZmUGlcAE1-47 lacking the transmembrane domain
7.4 - 7.6
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recombinant AtUGlcAE1DELTA1-64
8.5
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epimerization of UDPglucuronate to UDPgalacturonate
7.6
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7.6
recombinant AtUGlcAE2, lacking the amino acid position 1-68; recombinant AtUGlcAE3, lacking the amino acid position 1-53
7.6
recombinant OsUGlcAE3, lacking the amino acid position 1-53
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4 - 10
the activity of ZmUGlcAE1-47 is completely abolished when assays are conducted at pH value below 4 or above 10
5 - 8.9
pH 5.0: about 75% of maximal activity, pH 8.9: 93% of maximal activity
5 - 9
pH 5.0: about 65% of maximal activity, pH 9.0: about 95% of maximal activity
6.5 - 10
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pH 6.5: about 50% of maximal activity, pH 10.0: about 25% of maximal activity
7 - 10
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about 50% of maximal activity at pH 7 and 10, epimerization of UDPglucuronate to UDPgalacturonate
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30 - 42
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recombinant AtUGlcAE1DELTA1-64
37
assay at; recombinant AtUGlcAE2, lacking the amino acid position 1-68; recombinant AtUGlcAE2, lacking the amino acid position 1-68
37
recombinant OsUGlcAE3, lacking the amino acid position 1-53
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brenda
; GAE1; GAE2
brenda
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isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
brenda
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isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
brenda
only detected after pollen maturation
brenda
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brenda
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enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
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enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
; GAE1; GAE2
brenda
strong expression
brenda
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brenda
GAE1; GAE2; only in leaf veins
brenda
moderate expression; strong expression
brenda
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brenda
expressed in root hair zone; expression of GAE4 is confined to root tips; GAE1 is expressed throughout the root; GAE2 is expressed throughout the root; GAE3 is expressed in root hair zone
brenda
strong expression
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
; GAE1; GAE2
brenda
moderate expression; strong expression
brenda
; GAE1; GAE2
brenda
strong expression
brenda
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brenda
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differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
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differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
additional information
moderate expression throughout the plant; moderate expression throughout the plant; moderate expression throughout the plant; no expression in root or inflorescence
brenda
additional information
moderate expression throughout the plant; moderate expression throughout the plant; moderate expression throughout the plant; no expression in root or inflorescence
brenda
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exclusively localized in microsomal fraction, anchored to membrane
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brenda
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40000
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2 * 40000, SDS-PAGE
42900
2 * 42900, recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
44100
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
44300
2 * 44300, recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
45500
2 * 45500, recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
81400
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
88000
-
recombinant AtUGlcAE1DELTA1-64, gel filtration
88500
recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration; recombinant AtUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
92200
recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
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dimer
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2 * 43500
dimer
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration; 2 * 45500, recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
dimer
2 * 44300, recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
dimer
-
2 * 40000, SDS-PAGE
dimer
2 * 42900, recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
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-20 - 65
the activity of ZmUGlcAE lacking the putative transmembrane domain is completely abolished when assays are conducted at pH value below 4 or above 10, or when the assay temperature is above 65°C
25
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60 min, about 35% loss of activity
30
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60 min, about 50% loss of activity
37
-
60 min, about 75% loss of activity
42
-
60 min, about 20% loss of activity
-20
recombinant enzyme is still fully active after 1 year in storage
-20
recombinant enzyme ZmUGlcAE lacking the putative transmembrane domain is stable (more than 6 months) when stored as a crude extract at 20°C
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freezing and thawing of the crude extract in absence of cryoprotectants abolishes enzymatic activity entirely
KCl or NaCl, above 300 mM, completly inactivates the enzyme, when stored at -20°C for 2 weeks
-
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-10°C, stable for at least 1 year
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-20°C or -80°C in 50% v/v glycerol, 7 days, enzyme retains approximately 80% of its activity
-20°C, recombinant enzyme ZmUGlcAE lacking the putative transmembrane domain is stable (more than 6 months) when stored as a crude extract
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by using gel filtration and anion exchange chromatography
by using gel filtration and anion exchange chromatography; by using gel filtration and anion exchange chromatography; by using gel filtration and anion exchange chromatography
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
partial, AtUGlcAE1DELTA1-64 expressed in Escherichia coli
-
-
-
by using gel filtration and anion exchange chromatography
by using gel filtration and anion exchange chromatography
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
-
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
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expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression in Pichia pastoris
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isoform GAE3 is expressed in Escherichia coli BL21(DE3) cells
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isoform GAE6 is expressed in Escherichia coli BL21(DE3) cells
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no recovery of active recombinant enzyme when full-length AtUGlcAE1 is expressed in Escherichia coli due to the hydrophobic domain that results in un- or misfolded protein in inclusion bodies within Escherichia coli. Recombinant AtUGlcAE1DELTA1-64, lacking the putative transmembrane domain, can be expressed in Escherichia coli
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overexpression in Escherichia coli
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recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, is expressed in Escherichia coli
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GAE mRNA level decreases after Fusarium oxysporum infection
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DELTA1-47
recombinant product ZmUGlcAE, lacking the putative transmembrane domain, converts UDP-glucuronic acid to UDP-alpha-D-galacturonic acid while control Escherichia coli cells containing empty vector have no enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dalessandro, G.; Northcote, D.H.
Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in pine and fir
Biochem. J.
162
281-288
1977
Abies grandis, Pinus sylvestris
brenda
Bolwell, G.P.; Dalessandro, G.; Northcote, D.H.
Decrease of polygalacturonic acid synthase during xylem differentiation in sycamore
Phytochemistry
24
699-702
1985
Acer pseudoplatanus
-
brenda
Maitra, U.S.; Gaunt, M.A.; Ankel, H.
The mechanism of uridine diphosphate sugar-4-epimerase reactions. Isotope discrimination with 4-tritiated substrates
J. Biol. Chem.
249
3075-3078
1974
Dolichospermum flos-aquae
brenda
Gaunt, M.A.; Maitra, U.S.; Ankel, H.
Uridine diphosphate galacturonate 4-epimerase from the blue-green alga Anabaena flos-aquae
J. Biol. Chem.
249
2366-2372
1974
Dolichospermum flos-aquae
brenda
Davidson, E.A.
UDP-D-galacturonic acid 4-epimerase from radish roots
Methods Enzymol.
8
276-277
1966
Raphanus sativus
-
brenda
Feingold, D.S.; Neufeld, E.F.; Hassid, W.Z.
The 4-epimerization and decarboxylation of uridine diphosphate D-glucuronic acid by extracts from Phaseolus aureus seedlings
J. Biol. Chem.
235
910-913
1960
Vigna radiata var. radiata
brenda
Munoz, R.; Lopez, R.; De Frutos, M.; Garcia, E.
First molecular characterization of a uridine diphosphate galacturonate 4-epimerase: an enzyme required for capsular biosynthesis in Streptococcus pneumoniae type 1
Mol. Microbiol.
31
703-713
1999
Streptococcus pneumoniae
brenda
Usadel, B.; Schluter, U.; Molhoj, M.; Gipmans, M.; Verma, R.; Kossmann, J.; Reiter, W.D.; Pauly, M.
Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis
FEBS Lett.
569
327-331
2004
Arabidopsis thaliana, Arabidopsis thaliana (Q9LIS3)
brenda
Molhoj, M.; Verma, R.; Reiter, W.D.
The biosynthesis of D-galacturonate in plants. functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis
Plant Physiol.
135
1221-1230
2004
Arabidopsis thaliana (O22141), Arabidopsis thaliana (Q67ZJ4), Arabidopsis thaliana (Q9M0B6), Arabidopsis thaliana (Q9STI6)
brenda
Gu, X.; Bar-Peled, M.
The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-D-glucuronic acid 4-epimerase
Plant Physiol.
136
4256-4264
2004
Arabidopsis thaliana (O22141)
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (O22141), Arabidopsis thaliana (O81312), Arabidopsis thaliana (Q9LIS3), Arabidopsis thaliana (Q9LPC1), Arabidopsis thaliana (Q9M0B6), Arabidopsis thaliana (Q9STI6)
brenda
Gu, X.; Wages, C.; Davis, K.; Guyett, P.; Bar-Peled, M.
Enzymatic characterization and comparison of various poaceae UDP-GlcA 4-epimerase isoforms
J. Biochem.
146
527-534
2009
Arabidopsis thaliana (O22141), Arabidopsis thaliana (Q9LIS3), Arabidopsis thaliana (Q9M0B6), Oryza sativa, Oryza sativa (Q6K9M5), Zea mays (Q304Y2), Zea mays
brenda
Pang, C.Y.; Wang, H.; Pang, Y.; Xu, C.; Jiao, Y.; Qin, Y.M.; Western, T.L.; Yu, S.X.; Zhu, Y.X.
Comparative proteomics indicates that biosynthesis of pectic precursors is important for cotton fiber and Arabidopsis root hair elongation
Mol. Cell. Proteomics
9
2019-2033
2010
Arabidopsis thaliana, Gossypium hirsutum
brenda
Wojtasik, W.; Kulma, A.; Kostyn, K.; Szopa, J.
The changes in pectin metabolism in flax infected with Fusarium
Plant Physiol. Biochem.
49
862-872
2011
Linum usitatissimum
brenda
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