Information on EC 2.7.1.43 - glucuronokinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.43
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RECOMMENDED NAME
GeneOntology No.
glucuronokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-glucuronate = ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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Ascorbate and aldarate metabolism
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Metabolic pathways
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Pentose and glucuronate interconversions
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UDP-alpha-D-glucuronate biosynthesis (from myo-inositol)
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-glucuronate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-62-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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
ATP + D-galacturonate
P: ADP + 1-phospho-alpha-D-galacturonate
show the reaction diagram
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31% yield
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?
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
ATP + D-mannuronate
ADP + 1-phospho-alpha-D-mannuronate
show the reaction diagram
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95% yield
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?
D-glucuronic acid + ATP
D-glucuronic acid 1-phosphate + ADP
show the reaction diagram
dATP + D-glucuronate
dADP + 1-phospho-D-glucuronate
show the reaction diagram
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3% of the activity with ATP
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?
ITP + D-glucuronate
IDP + 1-phospho-D-glucuronate
show the reaction diagram
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3% of the activity with ATP
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?
additional information
?
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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
ATP + D-glucuronate
ADP + 1-phospho-alpha-D-glucuronate
show the reaction diagram
ATP + D-glucuronate
ADP + 1-phospho-D-glucuronate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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competitive to ATP
AMP
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with ATP as substrate
beta-D-glucuronic acid 1-phosphate
CDP
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with ATP as substrate
dATP
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with ATP as substrate
GDP
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with ATP as substrate
GTP
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with ATP as substrate
ITP
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with ATP as substrate
Tris-HCl
75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5
TTP
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with ATP as substrate
UDP
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with ATP as substrate
UDP-D-glucuronate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.059 - 1.9
ATP
0.031 - 0.7
D-glucuronate
0.62 - 0.697
D-glucuronic acid
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.5
ATP
Arabidopsis thaliana
Q93ZC9, Q9LY82
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8.3
D-glucuronic acid
Arabidopsis thaliana
Q93ZC9, Q9LY82
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
beta-D-glucuronic acid 1-phosphate
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pH 7.2, 30C
0.55
UDP-D-glucuronate
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pH 7.2, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.46
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pH 7.2, 30C
12.2
substrate: D-glucuronic acid
17.9
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after about 688fold purification; purified native enzyme, pH 7.5, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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no activity is measured below pH 4.5, whereas the maximum is reached between pH 7.5 and 8 with a far lower activity above pH 8.5
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9.5
no activity at pH 4.0, maximum at pH 7.5, low activity above pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
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temperatures above 45C lead to rapid inactivation of the enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
; 10% of maximal activity at 55C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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peptide sequencing from purified enzyme and mapping
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 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
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; 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
partial purification
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Protino-Ni1000 column chromatography and Strep-Tactin Macro Prep resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
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
expressed in Escherichia coli BL21(DE3) cells and Nicotiana benthamiana leaves
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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nonradioactive activity measurement by high-performance liquid chromatography