Information on EC 5.1.3.5 - UDP-arabinose 4-epimerase

Word Map on EC 5.1.3.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
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: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
5.1.3.5
-
RECOMMENDED NAME
GeneOntology No.
UDP-arabinose 4-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-L-arabinose = UDP-D-xylose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Metabolic pathways
-
-
UDP-beta-L-arabinose biosynthesis I (from UDP-alpha-D-xylose)
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-L-arabinose 4-epimerase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-18-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-xylopyranose
UDP-beta-L-arabinopyranose
show the reaction diagram
UDP-beta-L-arabinopyranose
UDP-alpha-D-xylopyranose
show the reaction diagram
-
-
-
r
UDP-D-xylopyranose
UDP-beta-L-arabinopyranose
show the reaction diagram
-
-
-
r
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-Chloromercuriphenylsulfonate
-
inhibition is reversed by Cys
p-hydroxymercuribenzoate
-
-
UDP
15% residual activity at 2 mM
UTP
54% residual activity at 2 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
150% activity at 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.015 - 1.5
UDP-D-xylose
0.016 - 0.5
UDP-L-arabinose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 13
UDP-alpha-D-xylopyranose
1.5
UDP-beta-L-arabinopyranose
Hordeum vulgare
Q2LC81, Q2LC82, Q2LC83
pH 7.0, at 25°C
13
UDP-D-xylopyranose
Sinorhizobium meliloti
Q92WA3
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
0.2 - 19
UDP-D-xylose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 42.1
UDP-alpha-D-xylopyranose
11720
1.1
UDP-beta-L-arabinopyranose
Hordeum vulgare
Q2LC81, Q2LC82, Q2LC83
pH 7.0, at 25°C
5012
42.1
UDP-D-xylopyranose
Sinorhizobium meliloti
Q92WA3
apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6
27264
0.5 - 45
UDP-D-xylose
341
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
native protein, substrate is UDP-arabinose; native protein, substrate is UDP-xylose
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
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
about pH 7.0; about pH 7.0; about pH 7.0
7.6
in phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
6: about 30% of maximal activity, 10: about 40% of maximal activity
8.5 - 9
maximum activity of recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
maximum activity of recombinant enzyme
25
assay at; assay at; assay at; assay at
30
maximum activity of native enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
66000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 36700, calculated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
approximately 3% w/w of the protein consists of fatty acids
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
recombinant Pisum enzyme loses both activities completely at temperatures higher than 40°C
50
-
1 min, 80% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, stable for at least 3 weeks, 50% loss of activity after 2 months
-
4°C, purified enzyme, at least 1 week, little or no loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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; 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 Arabidopsis enzyme by Ni-NTA affinity chromatography; purification of the recombinant Arabidopsis enzyme by Ni-NTA affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
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 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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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; 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
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