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Literature summary for 2.7.2.3 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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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

Cofactor

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