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Literature summary extracted from

  • Joao, H.C.; Williams, R.J.P.
    The anatomy of a kinase and the control of phosphate transfer (1993), Eur. J. Biochem., 216, 1-18.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.2.3 (NH4)2SO4 inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 ATP4- inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 Sodium citrate inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 Sodium selenate inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 Sodium succinate inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.3 (NH4)2SO4 inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 1,3-bisphosphoglycerate
-
 Equus caballus
2.7.2.3 1,3-bisphosphoglycerate
-
 Saccharomyces cerevisiae
2.7.2.3 1,3-bisphosphoglycerate
-
 Sus scrofa
2.7.2.3 3-phospho-D-glycerate
-
 Equus caballus
2.7.2.3 3-phospho-D-glycerate
-
 Saccharomyces cerevisiae
2.7.2.3 3-phospho-D-glycerate
-
 Sus scrofa
2.7.2.3 ATP4-
-
 Equus caballus
2.7.2.3 ATP4- inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 ATP4-
-
 Sus scrofa
2.7.2.3 gallic acid
-
 Equus caballus
2.7.2.3 gallic acid
-
 Saccharomyces cerevisiae
2.7.2.3 gallic acid
-
 Sus scrofa
2.7.2.3 inositol triphosphate
-
 Equus caballus
2.7.2.3 inositol triphosphate
-
 Saccharomyces cerevisiae
2.7.2.3 inositol triphosphate
-
 Sus scrofa
2.7.2.3 KH2PO4 inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 MK-401
-
 Equus caballus
2.7.2.3 MK-401
-
 Saccharomyces cerevisiae
2.7.2.3 MK-401
-
 Sus scrofa
2.7.2.3 NaCl inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 NaNO2 inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 phosphate
-
 Equus caballus
2.7.2.3 phosphate
-
 Saccharomyces cerevisiae
2.7.2.3 phosphate
-
 Sus scrofa
2.7.2.3 SO42-
-
 Equus caballus
2.7.2.3 SO42-
-
 Saccharomyces cerevisiae
2.7.2.3 SO42-
-
 Sus scrofa
2.7.2.3 Sodium citrate inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 Sodium selenate inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 Sodium succinate inhibition at high concentration, activation at low concentrations Saccharomyces cerevisiae
2.7.2.3 sulphasalazine
-
 Equus caballus
2.7.2.3 sulphasalazine
-
 Saccharomyces cerevisiae
2.7.2.3 sulphasalazine
-
 Sus scrofa
2.7.2.3 [Co(CN)6]3-
-
 Equus caballus
2.7.2.3 [Co(CN)6]3-
-
 Saccharomyces cerevisiae
2.7.2.3 [Co(CN)6]3-
-
 Sus scrofa
2.7.2.3 [Fe(CN)6]3-
-
 Equus caballus
2.7.2.3 [Fe(CN)6]3-
-
 Saccharomyces cerevisiae
2.7.2.3 [Fe(CN)6]3-
-
 Sus scrofa
2.7.2.3 [Fe(CN)6]4-
-
 Equus caballus
2.7.2.3 [Fe(CN)6]4-
-
 Saccharomyces cerevisiae
2.7.2.3 [Fe(CN)6]4-
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.3 additional information
-
 additional information kinetics Sus scrofa
2.7.2.3 additional information
-
 additional information kinetics Saccharomyces cerevisiae
2.7.2.3 additional information
-
 additional information kinetics Equus caballus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.3 KH2PO4 inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 Mg2+ required Sus scrofa
2.7.2.3 Mg2+ required Saccharomyces cerevisiae
2.7.2.3 Mg2+ required Equus caballus
2.7.2.3 Mg2+ true substrate is the magnesium complexes of ATP Sus scrofa
2.7.2.3 Mg2+ true substrate is the magnesium complexes of ATP Saccharomyces cerevisiae
2.7.2.3 Mg2+ true substrate is the magnesium complexes of ATP Equus caballus
2.7.2.3 NaCl inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
2.7.2.3 NaNO2 inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate Sus scrofa responsible for production of ATP during glycolysis ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate Saccharomyces cerevisiae responsible for production of ATP during glycolysis ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate Equus caballus responsible for production of ATP during glycolysis ATP + 3-phospho-D-glycerate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.3 Equus caballus
-
-
-
2.7.2.3 Saccharomyces cerevisiae
-
 normal and various site-specific mutant forms
-
2.7.2.3 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate mechanism Sus scrofa
a
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate mechanism Saccharomyces cerevisiae
a
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate mechanism Equus caballus
a
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate substrate binding Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate responsible for production of ATP during glycolysis Sus scrofa ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate responsible for production of ATP during glycolysis Saccharomyces cerevisiae ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate responsible for production of ATP during glycolysis Equus caballus ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Sus scrofa ADP + 1,3-diphosphoglycerate
-
 r
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Saccharomyces cerevisiae ADP + 1,3-diphosphoglycerate
-
 r
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Equus caballus ADP + 1,3-diphosphoglycerate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.2.3 More
-
 Sus scrofa
2.7.2.3 More overview: structure functioin relationship Saccharomyces cerevisiae
2.7.2.3 More overview: structure functioin relationship Equus caballus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.2.3 additional information
-
-
 Sus scrofa
2.7.2.3 additional information
-
-
 Equus caballus
2.7.2.3 additional information
-
 thermal analysis Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.3 ADP
-
 Sus scrofa
2.7.2.3 ADP true substrate is the magnesium complexes of ADP Saccharomyces cerevisiae
2.7.2.3 ADP true substrate is the magnesium complexes of ADP Equus caballus
2.7.2.3 ATP true substrate is the magnesium complexes of ATP Sus scrofa
2.7.2.3 ATP true substrate is the magnesium complexes of ATP Saccharomyces cerevisiae
2.7.2.3 ATP true substrate is the magnesium complexes of ATP Equus caballus
2.7.2.3 ATP required as phosphate donor Sus scrofa
2.7.2.3 ATP required as phosphate donor Saccharomyces cerevisiae
2.7.2.3 ATP required as phosphate donor Equus caballus