Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.2.3 extracted from

  • Larsson-Raznikiewicz, M.; Schierbeck, B.
    Activation and inhibition of the phosphoglycerate kinase reaction by ATP (1977), Biochim. Biophys. Acta, 481, 283-287.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP4- inhibition at high concentration, acceleration of activity at low concentrations Saccharomyces cerevisiae
ATP4- binds to the free enzyme as an inhibitor, when binding to the enzyme-MgATP2-(3-phospho-D-glycerate)complex, ATP4- acts as an activator Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
ATP4- binds to the free enzyme as an inhibitor, when binding to the enzyme-MgATP2-(3-phospho-D-glycerate)complex, ATP4- acts as an activator Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Mg2+ true substrate is the magnesium complexes of ATP Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
-
Saccharomyces cerevisiae ADP + 1,3-diphosphoglycerate
-
r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Saccharomyces cerevisiae

Cofactor

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