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Literature summary extracted from

  • Benziman, M.
    Pyruvate, orthophosphate dikinase from Acetobacter xylinum (1975), Methods Enzymol., 42C, 192-199.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.9.1 AMP phosphoenolpyruvate formation, competitive to ATP Komagataeibacter xylinus
2.7.9.1 ATP pyruvate formation, competitive to AMP Komagataeibacter xylinus
2.7.9.1 p-hydroxymercuribenzoate
-
 Komagataeibacter xylinus
2.7.9.1 potassium fluoride inhibits reaction in both directions at 50 mM Komagataeibacter xylinus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.9.1 0.0016
-
 AMP pH 6.5, 30ºC, pyruvate formation Komagataeibacter xylinus
2.7.9.1 0.06
-
 diphosphate pH 6.5, 30ºC, pyruvate formation Komagataeibacter xylinus
2.7.9.1 0.1
-
 phosphoenolpyruvate pH 6.5, 30ºC, pyruvate formation Komagataeibacter xylinus
2.7.9.1 0.2
-
 pyruvate pH 8.2, 30ºC, phosphoenolpyruvate formation Komagataeibacter xylinus
2.7.9.1 0.4
-
 ATP pH 8.2, 30ºC, phosphoenolpyruvate formation Komagataeibacter xylinus
2.7.9.1 0.8
-
 phosphate pH 8.2, 30ºC, phosphoenolpyruvate formation Komagataeibacter xylinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.1 Mg2+
-
 Komagataeibacter xylinus
2.7.9.1 Mn2+ cannot replace Mg2+ in either the forward or the reverse reaction Komagataeibacter xylinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate Komagataeibacter xylinus enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation AMP + phosphoenolpyruvate + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 Komagataeibacter xylinus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.9.1 partial, using ammonium sulfate precipitation and chromatography on DEAE-cellulose Komagataeibacter xylinus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.9.1 0.88
-
-
 Komagataeibacter xylinus

Storage Stability

EC Number Storage Stability Organism
2.7.9.1 retains 85% of activity after two weeks at room temperature Komagataeibacter xylinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.1 ATP + pyruvate + arsenate the rate of phosphoenolpyruvate formation in the presence of arsenate is 65% lower than that obtained with phosphate Komagataeibacter xylinus ?
-
 ?
2.7.9.1 ATP + pyruvate + phosphate GTP, CTP, ITP or TTP cannot replace ATP in the reaction with pyruvate Komagataeibacter xylinus AMP + phosphoenolpyruvate + diphosphate GDP, CMP and ADP cannot replace AMP in the reverse reaction r
2.7.9.1 ATP + pyruvate + phosphate enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation Komagataeibacter xylinus AMP + phosphoenolpyruvate + diphosphate
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.9.1 30
-
 assay at Komagataeibacter xylinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.9.1 6.5
-
 pyruvate formation Komagataeibacter xylinus
2.7.9.1 8.2
-
 phosphoenolpyruvate formation Komagataeibacter xylinus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.9.1 0.2
-
 AMP pH 8.2, 30ºC, phosphoenolpyruvate formation Komagataeibacter xylinus
2.7.9.1 0.22
-
 ATP pH 6.5, 30ºC, pyruvate formation Komagataeibacter xylinus