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Literature summary extracted from

  • Shinagawa, E.; Adachi, O.; Ano, Y.; Yakushi, T.; Matsushita, K.
    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.
    View publication on PubMed

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