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Literature summary for 1.1.1.95 extracted from

  • Grant, G.A.; Hu, Z.; Xu, X.L.
    Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding (2002), J. Biol. Chem., 277, 39548-39553.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-Ser binding of the inhibitor to the apoenzyme displays positive cooperativity in the binding of the first two serine molecules and negative cooperativity in the binding of the last two serine molecules. At least two NADH-induced conformational forms of the enzyme bind the inhibitor in the physiological range. Successive binding of NADH to the enzyme results in an increase in the affinity for the first inhibitor ligand bound and a lessening of both the positive and negative cooperativity of inhibitor binding Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-ketoglutarate + NADH
-
Escherichia coli 2-hydroxyglutaric acid + NAD+
-
?

Cofactor

Cofactor Comment Organism Structure
NADH binding of 4 NADH per tetrameric enzyme, negative cooperativity in NADH binding Escherichia coli