Information on EC 5.4.99.30 - UDP-arabinopyranose mutase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.30
-
RECOMMENDED NAME
GeneOntology No.
UDP-arabinopyranose mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-arabinopyranose pyranomutase
The reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
show the reaction diagram
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-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
show the reaction diagram
O82706, Q8H8T0
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
5 mM, activity almost doubles; 5 mM, activity almost doubles
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
5 mM, complete inhibition; 5 mM, complete inhibition
UDP
competitive inhibition, lower affinity for enzyme than substrate
UDP-Gal
UDP-Glc
UDP-Xyl
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0531
beta-L-arabinofuranose
pH 6.8, 25°C; pH 6.8, 25°C
0.055
beta-L-arabinopyranose
pH 6.8, 25°C; pH 6.8, 25°C
0.0228 - 0.371
UDP-beta-L-arabinofuranose
0.0454 - 10.3
UDP-beta-L-arabinopyranose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.474 - 5.98
UDP-beta-L-arabinofuranose
0.185 - 1.44
UDP-beta-L-arabinopyranose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 39.3
UDP-beta-L-arabinofuranose
12087
0.09 - 40.8
UDP-beta-L-arabinopyranose
5012
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
UDP
pH 6.8, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
formation of beta-L-arabinofuranose; formation of beta-L-arabinofuranose
6.5
furanose-forming activity; furanose-forming activity
6.8
assay at; assay at; assay at
7 - 7.5
formation of beta-L-arabinopyranose; formation of beta-L-arabinopyranose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
pH 4.0: about 40% of maximal activity, pH 8.0: about 55% of maximal activity, pyranose forming activity; pH 4.0: about 40% of maximal activity, pH 8.0: about 55% of maximal activity, pyranose forming activity
5 - 8
pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity, furanose-forming activity; pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity, furanose-forming activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
30°C: about 50% of maximal activity, 60°C: about 85% of maximal activity; 30°C: about 50% of maximal activity, 60°C: about 85% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
almost exclusively detected in siliques, with the highest levels 6 to 8 d post anthesis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, SDS-PAGE; x * 40000, SDS-PAGE
40600
calculated from cDNA; calculated from cDNA
41000
x * 41000, SDS-PAGE; x * 41000, SDS-PAGE
41300
calculated from cDNA
41349
x * 41349, calculated from sequence; x * 41349, calculated from sequence
460000
mutase is likely to exist as a complex composed of numerous proteins, gel filtration; mutase is likely to exist as a complex composed of numerous proteins, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
80 h, 50% loss of activity; 80 h, 50% loss of activity
50
1 h, 50% loss of activity; 1 h, 50% loss of activity
60
-
enzymatic activity decreases to 24.5% after 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated cycles of freezing and thawing did not significantly affect mutase activity
-
rUMA1 expressed in insect cells retains activity after repeated cycles of freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, mutase activity is stable for at least 3 months
-
4°C, mutase activity is stable for 3 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified 94fold using hydrophobic chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein; expressed in Escherichia coli as a His-tagged fusion protein; expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli; expressed in Escherichia coli
expression in insect cells; expression in insect cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D112N
activity is 131% of wild-type activity
R149A
activity is 154.1% of wild-type activity
R151A
no activity
R156A
activity is 0.1% of wild-type activity
R158A
activity is 5.7% of wild-type activity
R163A
activity is 2.0% of wild-type activity
R165A
activity is 131% of wild-type activity
R165K
activity is 131% of wild-type activity