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Literature summary for 1.4.1.3 extracted from

  • Carrigan, J.B.; Engel, P.C.
    The structural basis of proteolytic activation of bovine glutamate dehydrogenase (2008), Protein Sci., 17, 1346-1353.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ADP ADP activation is almost abolished after treatment with TLCK-treated chymotrypsin Bos taurus
chymotrypsin 0.2 mg/ml chymotrypsin cleaves glutamate dehydrogenase in such a fashion as to cause a rise in activity with NADP+ and NAD+ as coenzyme, over threefold activation in the NADP+ assay with TLCK-treated chymotrypsin, the distinguishing aspect with untreated chymotrypsin is that the activation is followed by a decrease in activity Bos taurus
additional information not inhibited by trypsin Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
GTP GTP inhibition is attenuated to some extent by the proteolysis with TLCK-treated chymotrypsin 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 + H+
-
?

Synonyms

Synonyms Comment Organism
GDH
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bos taurus
NADP+
-
Bos taurus