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Literature summary for 2.7.1.43 extracted from
- Cloning of glucuronokinase from Arabidopsis thaliana, the last missing enzyme of the MIOX pathway to nucleotide sugars (2009), J. Biol. Chem., 285, 2902-2910.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning from Arabidopsis thaliana using the peptide sequences of Lillium longiflorum enzyme, DNA and amino acid sequence determination and analysis | Arabidopsis thaliana |
| 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 | Arabidopsis thaliana |
| His-tag, expressed in Escherichis coli XL-1 | Arabidopsis thaliana |
General Stability
| General Stability | Organism |
|---|---|
| 75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5 | Arabidopsis thaliana |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Tris-HCl | 75% decrease of enzyme activity in Tris-HCl buffer, pH 7.5, compared with MOPS-KOH buffer, pH 7.5 | Arabidopsis thaliana |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | allosteric enzyme, sigmoidal curve in kinetics with ATP | Arabidopsis thaliana | |
| 0.555 | - |
ATP | allosteric interaction (Hill coefficient: 1.54) | Arabidopsis thaliana | |
| 0.56 | - |
ATP | pH 7.5, 30°C, recombinant enzyme | Arabidopsis thaliana | |
| 0.62 | - |
D-glucuronic acid | - |
Lilium longiflorum | |
| 0.697 | - |
D-glucuronic acid | - |
Arabidopsis thaliana | |
| 0.7 | - |
D-glucuronate | pH 7.5, 30°C, recombinant enzyme | Arabidopsis thaliana | |
| 1.9 | - |
ATP | - |
Lilium longiflorum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates, can substitute for Mg2+ | Arabidopsis thaliana | |
| Mg2+ | required | Lilium longiflorum | |
| Mg2+ | required | Arabidopsis thaliana | |
| Mg2+ | Mn2+, Co2+, Ca2+ are able to substitute for Mg2+ (94%-44% relative activity) | Arabidopsis thaliana | |
| Mn2+ | activates, can substitute for Mg2+ | Arabidopsis thaliana | |
| additional information | slight activation by trivalent cations, no effect by monovalent cations | Arabidopsis thaliana |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
x * 40000 Da, SDS-PAGE | Lilium longiflorum |
| 40000 | - |
x * 40000, about, sequence calculation | Arabidopsis thaliana |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-glucuronate | Lilium longiflorum | - |
ADP + 1-phospho-alpha-D-glucuronate | - |
? | |
| ATP + D-glucuronate | Arabidopsis thaliana | - |
ADP + 1-phospho-alpha-D-glucuronate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q93ZC9 | - |
- |
| Arabidopsis thaliana | Q93ZC9 | glucuronokinase 1 | - |
| Arabidopsis thaliana | Q9LY82 | glucuronokinase 2 | - |
| Lilium longiflorum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Lilium longiflorum |
- |
Arabidopsis thaliana |
| 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 | Lilium longiflorum |
| recombinant His-tagged enzyme from Escherichiaa coli strain XL-1 Blue by nickel affinity chromatography | Arabidopsis thaliana |
| recombinant His6-tagged enzyme from Escherichia coli strain XL-1 Blue by nickel affinity chromatography | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | 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 | Arabidopsis thaliana | - |
| additional information | 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 | Arabidopsis thaliana | - |
| pollen | - |
Lilium longiflorum | - |
| pollen | - |
Arabidopsis thaliana | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 12.2 | - |
substrate: D-glucuronic acid | Arabidopsis thaliana |
| 12.6 | - |
substrate: ATP | Arabidopsis thaliana |
| 17.9 | - |
after about 688fold purification | Lilium longiflorum |
| 17.9 | - |
purified native enzyme, pH 7.5, 30°C | Lilium longiflorum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-glucuronate | - |
Lilium longiflorum | ADP + 1-phospho-alpha-D-glucuronate | - |
? | |
| ATP + D-glucuronate | - |
Arabidopsis thaliana | ADP + 1-phospho-alpha-D-glucuronate | - |
? | |
| D-glucuronic acid + ATP | - |
Lilium longiflorum | D-glucuronic acid 1-phosphate + ADP | - |
? | |
| D-glucuronic acid + ATP | D-glucose, D-xylose, L-arabinose, D-galactose, D-galacturonic acid, UTP, CTP, GTP, UDP, or ADP are not utilized as substrates | Arabidopsis thaliana | D-glucuronic acid 1-phosphate + ADP | - |
? | |
| additional information | 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 | Arabidopsis thaliana | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000 Da, SDS-PAGE | Lilium longiflorum |
| ? | x * 40000, about, sequence calculation | Arabidopsis thaliana |
| More | peptide sequencing from purified enzyme and mapping | Lilium longiflorum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlcAK | - |
Lilium longiflorum |
| GlcAK | - |
Arabidopsis thaliana |
| glucuronokinase | - |
Lilium longiflorum |
| glucuronokinase | - |
Arabidopsis thaliana |
| glucuronokinase 1 | - |
Arabidopsis thaliana |
| glucuronokinase 2 | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Lilium longiflorum |
| 35 | - |
- |
Arabidopsis thaliana |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 60 | - |
Arabidopsis thaliana |
| 10 | 60 | 10% of maximal activity at 55°C | Arabidopsis thaliana |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 8.3 | - |
D-glucuronic acid | - |
Arabidopsis thaliana | |
| 8.5 | - |
ATP | - |
Arabidopsis thaliana | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Arabidopsis thaliana |
| 7.5 | - |
assay at | Lilium longiflorum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9.5 | no activity at pH 4.0, maximum at pH 7.5, low activity above pH 8.0 | Arabidopsis thaliana |
| 5 | 9.5 | - |
Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Lilium longiflorum | |
| ATP | - |
Arabidopsis thaliana | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Arabidopsis thaliana | sequence calculation | - |
5.4 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | glucuronokinase is a member of the GHMP-kinase superfamily | Lilium longiflorum |
| evolution | glucuronokinase is a member of the GHMP-kinase superfamily | Arabidopsis thaliana |
| metabolism | the enzyme is involved in the the myo-inositol oxygenase pathway to nucleotide sugars, as part of the nucleotide sugar interconversion pathway, overview | Lilium longiflorum |
| metabolism | the enzyme is involved in the the myo-inositol oxygenase pathway to nucleotide sugars, as part of the nucleotide sugar interconversion pathway, overview | Arabidopsis thaliana |
| 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 | Lilium longiflorum |
| 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 | Arabidopsis thaliana |
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