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Literature summary extracted from
- Purification and characterization of membrane-bound 3-dehydroshikimate dehydratase from Gluconobacter oxydans IFO 3244, a new enzyme catalyzing extracellular protocatechuate formation (2010), Biosci. Biotechnol. Biochem., 74, 1084-1088.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.2.1.118 | MgCl2 partially stabilizes the cytosolic isozyme during purification | Gluconobacter oxydans |
| 4.2.1.118 | the membrane-bound isozyme is stable in contrast to the cytosolic isoform | Gluconobacter oxydans |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.118 | KCl | decreases mDSD enzyme activity during purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside | Gluconobacter oxydans |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.1.118 | 0.5 | - |
3-dehydroshikimate | pH 6.5, 25°C | Gluconobacter oxydans | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.1.10 | cytosol | cytosolic isozyme sDQD | Gluconobacter oxydans | 5829 | - |
| 4.2.1.10 | membrane | membrane-bound isoform mDQD | Gluconobacter oxydans | 16020 | - |
| 4.2.1.118 | membrane | membrane-bound isoform mDSD | Gluconobacter oxydans | 16020 | - |
| 4.2.1.118 | membrane | membrane-bound isoform mDSD | Gluconacetobacter liquefaciens | 16020 | - |
| 4.2.1.118 | membrane | membrane-bound isoform mDSD, the isozyme is stable in contrast to the cytosolic isoform, sDSD | Gluconobacter oxydans | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.10 | KCl | facilitates mDQD enzyme purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside as a chaotropic agent | Gluconobacter oxydans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.118 | 76000 | - |
mDSD, gel filtration | Gluconobacter oxydans |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.10 | 3-dehydroquinate | Gluconobacter oxydans | - |
3-dehydroshikimate + H2O | - |
? | |
| 4.2.1.10 | 3-dehydroquinate | Gluconobacter oxydans IFO 3244 | - |
3-dehydroshikimate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | Gluconobacter oxydans | - |
protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | Gluconacetobacter liquefaciens | - |
protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | Gluconobacter oxydans | mDSD is specific for 3-dehydroshikimate | protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | Gluconobacter oxydans IFO 3244 | - |
protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | Gluconobacter oxydans IFO 3244 | mDSD is specific for 3-dehydroshikimate | protocatechuate + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.10 | Gluconobacter oxydans | - |
- |
- |
| 4.2.1.10 | Gluconobacter oxydans IFO 3244 | - |
- |
- |
| 4.2.1.118 | Gluconacetobacter liquefaciens | - |
- |
- |
| 4.2.1.118 | Gluconobacter oxydans | - |
- |
- |
| 4.2.1.118 | Gluconobacter oxydans IFO 3244 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.118 | native mDSD from strain IFO 3244 membrane fraction to homogeneity by solubilization with detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside, anion exchange and hydroxyapatite chromatography. The cytosolic isozyme sDSD is purified from the cytosolic fraction after centrifugation at 62000 x g followed by anion echange chromatograohy, ammonium sulfate precipitation, and dialysis, the enzyme activity is lost during dialysis | Gluconobacter oxydans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.10 | 3-dehydroquinate | - |
Gluconobacter oxydans | 3-dehydroshikimate + H2O | - |
? | |
| 4.2.1.10 | 3-dehydroquinate | - |
Gluconobacter oxydans IFO 3244 | 3-dehydroshikimate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | - |
Gluconobacter oxydans | protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | - |
Gluconacetobacter liquefaciens | protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | mDSD is specific for 3-dehydroshikimate | Gluconobacter oxydans | protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | - |
Gluconobacter oxydans IFO 3244 | protocatechuate + H2O | - |
? | |
| 4.2.1.118 | 3-dehydroshikimate | mDSD is specific for 3-dehydroshikimate | Gluconobacter oxydans IFO 3244 | protocatechuate + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.118 | monomer | 1 * 76000, mSDS, SDS-PAGE | Gluconobacter oxydans |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.10 | 3-dehydroquinate dehydratase | - |
Gluconobacter oxydans |
| 4.2.1.10 | DQD | - |
Gluconobacter oxydans |
| 4.2.1.10 | mDQD | - |
Gluconobacter oxydans |
| 4.2.1.10 | membrane-bound 3-dehydroquinate dehydratase | - |
Gluconobacter oxydans |
| 4.2.1.118 | 3-dehydroshikimate dehydratase | - |
Gluconobacter oxydans |
| 4.2.1.118 | 3-dehydroshikimate dehydratase | - |
Gluconacetobacter liquefaciens |
| 4.2.1.118 | DSD | - |
Gluconobacter oxydans |
| 4.2.1.118 | DSD | - |
Gluconacetobacter liquefaciens |
| 4.2.1.118 | mDSD | - |
Gluconobacter oxydans |
| 4.2.1.118 | mDSD | - |
Gluconacetobacter liquefaciens |
| 4.2.1.118 | membrane-bound 3-dehydroshikimate dehydratase | - |
Gluconobacter oxydans |
| 4.2.1.118 | membrane-bound 3-dehydroshikimate dehydratase | - |
Gluconacetobacter liquefaciens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.118 | 25 | - |
assay at | Gluconobacter oxydans |
| 4.2.1.118 | 25 | - |
assay at | Gluconacetobacter liquefaciens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.118 | 47 | - |
sDSD activity is lost within min, MgCl2 partially stabilizes | Gluconobacter oxydans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.118 | 6 | 8 | - |
Gluconobacter oxydans |
| 4.2.1.118 | 6.5 | - |
assay at | Gluconobacter oxydans |
| 4.2.1.118 | 6.5 | - |
assay at | Gluconacetobacter liquefaciens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.118 | additional information | no cofactor requirement | Gluconobacter oxydans |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.118 | physiological function | 3-dehydroshikimate dehydratase is the first enzyme known to catalyze the aromatization of dehydroshikimate to protocatechuate | Gluconobacter oxydans |
| 4.2.1.118 | physiological function | 3-dehydroshikimate dehydratase is the first enzyme known to catalyze the aromatization of dehydroshikimate to protocatechuate | Gluconacetobacter liquefaciens |
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