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Literature summary for 1.4.1.3 extracted from

  • Di Prisco, G.
    Effect of pH and ionic strength on the catalytic and allosteric properties of native and chemically modified ox liver mitochondrial glutamate dehydrogenase (1975), Arch. Biochem. Biophys., 171, 604-612.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP above pH 7.0: allosteric activation Bos taurus
ADP pH 6.0-7.0: strong inhibition Bos taurus
GTP inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0 Bos taurus
phosphate activator at pH 8.0-9.0, inhibitor at pH 6.0-7.6 Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ADP above pH 7.0: allosteric activation, pH 6.0-7.0: strong inhibition Bos taurus
GTP inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0 Bos taurus
phosphate pH 8.0-9.0: activation, pH 6.0-7.6: almost complete inhibition with 400 mM Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD(P)+
-
Bos taurus 2-oxoglutarate + NH3 + NAD(P)H
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
in the absence of phosphate Bos taurus
9
-
in the presence of 330 mM phosphate Bos taurus