Information on EC 2.7.7.44 - glucuronate-1-phosphate uridylyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.44
-
RECOMMENDED NAME
GeneOntology No.
glucuronate-1-phosphate uridylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UTP + 1-phospho-alpha-D-glucuronate = diphosphate + UDP-glucuronate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Ascorbate and aldarate metabolism
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
UDP-alpha-D-glucuronate biosynthesis (from myo-inositol)
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:1-phospho-alpha-D-glucuronate uridylyltransferase
Also acts slowly with CTP.
CAS REGISTRY NUMBER
COMMENTARY hide
52228-05-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Soybean (L.) Merrill
SwissProt
Manually annotated by BRENDA team
var. Larker
-
-
Manually annotated by BRENDA team
Linne
-
-
Manually annotated by BRENDA team
Linne
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UTP + D-glucuronic acid 1-phosphate
?
show the reaction diagram
-
predominant route whereby UDPglucuronic acid is termed in young barley seedlings
-
-
?
UTP + D-glucuronic acid 1-phosphate
diphosphate + UDP-D-glucuronic acid
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
UTP + D-glucuronic acid 1-phosphate
?
show the reaction diagram
-
predominant route whereby UDPglucuronic acid is termed in young barley seedlings
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
36% of the activation with Mg2+
Co2+
-
40% of the activation with Mg2+
Mn2+
-
can substitute for Mg2+ in either the forward or the reverse direction, 53% of the activation with Mg2+, excess of Mn2+ inhibits the reaction in both directions
Zn2+
-
37% of the activation with Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
-
best fulfills the requirement for a divalent cation, maximal activity of forward reaction at a Mg2+/UTP ratio of 2:1. In the reverse reaction below 5 mM diphosphate, a Mg2+:diphosphate ratio of approximately 1:1 gives optimal activity, excess of Mg2+ is inhibitory
Mn2+
-
53% of the activation with Mg2+, excess of Mn2+ inhibits the reaction in both directions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
alpha-D-glucose 1-phosphate
-
0.14
alpha-D-glucuronic acid 1-phosphate
-
0.33
D-glucuronic acid 1-phosphate
-
pH 8.0, 30°C
0.5
UDP-D-glucuronic acid
-
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0019
substrate alpha-D-mannose 1-phosphate
0.0022
substrate D-glucose 6-phosphate
0.0034
substrate N-acetyl-alpha-D-glucosamine 1-phosphate
0.097
substrate alpha-D-glucoronic acid 1-phosphate
0.11
substrate alpha-D-glucose 1-phosphate
0.112
substrate alpha-D-galactose 1-phosphate
additional information
UDP-GlcA PPase activity increases 3.9fold during embryo development (25-45 daf), the activity increases in proportion to the increase in seed fresh weight during embryo development
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
broad pH optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
synchronous
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, if dialyzed and stored deep frozen the enzyme rapidly loses activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-Link affinity resin
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli