Information on EC 2.7.1.43 - glucuronokinase

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The expected taxonomic range for this enzyme is: Magnoliophyta

EC NUMBER
COMMENTARY
2.7.1.43
-
RECOMMENDED NAME
GeneOntology No.
glucuronokinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + D-glucuronate = ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
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
ATP:D-glucuronate 1-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
GlcAK
Q93ZC9, Q9LY82
-
glucuronokinase
Q93ZC9
-
glucuronokinase
-
-
glucuronokinase 1
Q93ZC9
-
glucuronokinase 2
Q9LY82
-
glucuronokinase, glucurono-
-
-
-
-
kinase, glucurono- (phosphorylating)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-62-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; glucuronokinase 1
UniProt
Manually annotated by BRENDA team
glucuronokinase 2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-, Q93ZC9, Q9LY82
glucuronokinase is a member of the GHMP-kinase superfamily; glucuronokinase is a member of the GHMP-kinase superfamily
evolution
-
glucuronokinase is a member of the GHMP-kinase superfamily
metabolism
-, Q93ZC9, Q9LY82
the enzyme is involved in the the myo-inositol oxygenase pathway to nucleotide sugars, as part of the nucleotide sugar interconversion pathway, overview; the enzyme is involved in the the myo-inositol oxygenase pathway to nucleotide sugars, as part of the nucleotide sugar interconversion pathway, overview
metabolism
-
the enzyme is involved in the the myo-inositol oxygenase pathway to nucleotide sugars, as part of the nucleotide sugar interconversion pathway, overview
physiological function
-, Q93ZC9, Q9LY82
nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls, the main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate; nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls, the main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate
physiological function
-
nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls, the main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
r
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-, ?
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-, ?
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-, ?
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
?
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
-
-
-
-
?
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
Q93ZC9, Q9LY82
-
-
-
?
D-glucuronic acid + ATP
D-glucuronic acid 1-phosphate + ADP
show the reaction diagram
-
-
-
-
?
D-glucuronic acid + ATP
D-glucuronic acid 1-phosphate + ADP
show the reaction diagram
-, Q93ZC9, Q9LY82
D-glucose, D-xylose, L-arabinose, D-galactose, D-galacturonic acid, UTP, CTP, GTP, UDP, or ADP are not utilized as substrates
-
-
?
dATP + D-glucuronate
dADP + 1-phospho-D-glucuronate
show the reaction diagram
-
3% of the activity with ATP
-
-
?
ITP + D-glucuronate
IDP + 1-phospho-D-glucuronate
show the reaction diagram
-
3% of the activity with ATP
-
-
?
additional information
?
-
-
less than 1% of the activity with ATP: GTP, CTP, UTP, TTP
-
-
-
additional information
?
-
-
no substrate: UTP, GTP, CTP
-
-
-
additional information
?
-
-, Q93ZC9, Q9LY82
the enzyme is absolutely specific for D-glucuronate and ATP, no activity with D-glucose, D-xylose, L-arabinose, D-galactose, or D-galacturonic acid as acceptor substrate or with UTP, CTP, GTP, UDP, and ADP as donor substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
-
-
-
-
-
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
-
-
-
-
?
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
Q93ZC9, Q9LY82
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-, Q93ZC9, Q9LY82
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can partially replace Mg2+ in activation
Co2+
-, Q93ZC9, Q9LY82
activates, can substitute for Mg2+
Mg2+
-
divalent cation required, Mg2+ most effective
Mg2+
-, Q93ZC9, Q9LY82
Mn2+, Co2+, Ca2+ are able to substitute for Mg2+ (94%-44% relative activity); required; required
Mg2+
-
required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-, Q93ZC9, Q9LY82
activates, can substitute for Mg2+
additional information
-, Q93ZC9, Q9LY82
slight activation by trivalent cations, no effect by monovalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
competitive to ATP
AMP
-
with ATP as substrate
beta-D-glucuronic acid 1-phosphate
-
50% inhibition at 1-3 mM
beta-D-glucuronic acid 1-phosphate
-
-
CDP
-
with ATP as substrate
dATP
-
with ATP as substrate
GDP
-
with ATP as substrate
GTP
-
with ATP as substrate
ITP
-
with ATP as substrate
Tris-HCl
-, Q93ZC9, Q9LY82
75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5
TTP
-
with ATP as substrate
UDP
-
with ATP as substrate
UDP-D-glucuronate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.555
-
ATP
-, Q93ZC9, Q9LY82
allosteric interaction (Hill coefficient: 1.54)
0.56
-
ATP
-, Q93ZC9, Q9LY82
pH 7.5, 30C, recombinant enzyme
1.9
-
ATP
-
pH 7.2, 30C
0.5
0.6
D-glucuronate
-
pH 7.2, 30C
0.7
-
D-glucuronate
-, Q93ZC9, Q9LY82
pH 7.5, 30C, recombinant enzyme
0.62
-
D-glucuronic acid
-
-
0.697
-
D-glucuronic acid
-, Q93ZC9, Q9LY82
-
additional information
-
additional information
-, Q93ZC9, Q9LY82
allosteric enzyme, sigmoidal curve in kinetics with ATP
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.5
-
ATP
-, Q93ZC9, Q9LY82
-
8.3
-
D-glucuronic acid
-, Q93ZC9, Q9LY82
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.18
-
beta-D-glucuronic acid 1-phosphate
-
pH 7.2, 30C
0.55
-
UDP-D-glucuronate
-
pH 7.2, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.46
-
-
pH 7.2, 30C
12.2
-
-, Q93ZC9, Q9LY82
substrate: D-glucuronic acid
12.6
-
-, Q93ZC9, Q9LY82
substrate: ATP
17.9
-
-
after about 688fold purification; purified native enzyme, pH 7.5, 30C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-, Q93ZC9, Q9LY82
-
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9.5
-, Q93ZC9, Q9LY82
no activity at pH 4.0, maximum at pH 7.5, low activity above pH 8.0
5
9.5
-, Q93ZC9, Q9LY82
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-, Q93ZC9, Q9LY82
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
60
-, Q93ZC9, Q9LY82
; 10% of maximal activity at 55C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-, Q93ZC9, Q9LY82
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q93ZC9, Q9LY82
;
Manually annotated by BRENDA team
additional information
-, Q93ZC9, Q9LY82
in Arabidopsis, the enzyme is expressed in all tissues with a preference for pollen. The expresseion level of glucuronokinase 1 is about 15fold higher than of glucuronokinase 2; in Arabidopsis, the enzyme is expressed in all tissues with a preference for pollen. The expression level of glucuronokinase 1 is about 15fold higher than of glucuronokinase 2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q93ZC9, Q9LY82
x * 40000, about, sequence calculation
?
-
x * 40000 Da, SDS-PAGE
additional information
-
peptide sequencing from purified enzyme and mapping
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5
-, Q93ZC9, Q9LY82
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; recombinant His6-tagged enzyme from Escherichia coli strain XL-1 Blue by nickel affinity chromatography; recombinant His-tagged enzyme from Escherichiaa coli strain XL-1 Blue by nickel affinity chromatography
-, Q93ZC9, Q9LY82
; native enzyme 688.5fold from pollen by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration followed by ultrafiltration, affinity chromatography, and another step of anion exchange chromatography, and hydrophobic interaction chromatography
-
partial purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning from Arabidopsis thaliana using the peptide sequences of Lillium longiflorum enzyme, DNA and amino acid sequence determination and analysis; cloning from Arabidopsis thaliana using the peptide sequences of Lillium longiflorum enzyme, DNA and amino acid sequence determination and analysis, expression as His6-tagged protein in Escherichia coli strain XL-1 Blue; His-tag, expressed in Escherichis coli XL-1
-, Q93ZC9, Q9LY82
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
nonradioactive activity measurement by high-performance liquid chromatography