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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase and Organism(s) Pisum sativum and UniProt Accession B0M3E8

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.2 UDP-glucose 4-epimerase
IUBMB Comments
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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This record set is specific for:
Pisum sativum
UNIPROT: B0M3E8
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-Glc 4-epimerase
-
UDP-glucose 4-epimerase
-
UDP-Xyl 4-epimerase
-
UDP-xylose 4-epimerase
-
4-Epimerase
-
-
-
-
Epimerase, uridine diphosphoglucose
-
-
-
-
Galactowaldenase
-
-
-
-
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-galactose 4-epimerase
-
-
-
-
UDP-glucose epimerase
-
-
-
-
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
-
-
-
-
Uridine diphosphate glucose 4-epimerase
-
-
-
-
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
additional information
PsUGE1 belongs to plant UGE I family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-89-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
-
-
-
r
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-L-arabinose
UDP-D-xylose
show the reaction diagram
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
-
-
-
r
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
-
-
-
r
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
complete inhibition, recombinan t enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
recombinant enzyme
8.6
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
maximum activity of recombinant PsUGE1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UGE1_PEA
350
0
38960
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
x * 38994, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 38994, calculation from nucleotide sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team