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Literature summary for 2.7.2.3 extracted from

  • Ali, M.; Brownstone, Y.S.
    A study of phosphoglycerate kinase in human erythrocytes. II. Kinetic properties (1976), Biochim. Biophys. Acta, 445, 89-103.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
1,3-diphosphoglycerate substrate activation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2,3-diphosphoglycerate noncompetitive with respect to 1,3-diphosphoglycerate Homo sapiens
AMP noncompetitive with respect to 1,3-diphosphoglycerate, ADP and Mg2+, inhibition kinetics Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
ADP
-
Homo sapiens
ATP required as phosphate donor Homo sapiens