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Literature summary for 1.4.1.3 extracted from

  • McCarthy, A.D.; Tipton, K.F.
    Ox glutamate dehydrogenase. Comparison of the kinetic properties of native and proteolysed preparations (1985), Biochem. J., 230, 95-99.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ADP 1.5fold activation, 0.08 mM NADH as cofactor Bos taurus
ATP 4.8fold activation, cofactor 0.08 mM NADH Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
GTP
-
Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
NADPH
-
Bos taurus
0.02
-
NADH
-
Bos taurus
0.36
-
2-oxoglutarate NADH + NH4Cl Bos taurus
0.47
-
2-oxoglutarate NADPH + NH4Cl Bos taurus
1
-
L-glutamate 1 mM, NAD+ Bos taurus
3
-
L-glutamate 1 mM, NADP+ Bos taurus
25
-
L-glutamate 0.004 mM, NAD+ Bos taurus
44
-
NH3 NADPH + 2-oxoglutarate Bos taurus
50
-
NH3 NADH + 2-oxoglutarate Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Bos taurus
-
liver
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NADH + NH3
-
Bos taurus L-glutamate + NAD+ + H2O
-
?
2-oxoglutarate + NH3 + NADH + H+ NH4Cl used in enzyme assay Bos taurus L-glutamate + H2O + NAD+
-
r
2-oxoglutarate + NH3 + NADPH + H+ NH4Cl used in enzyme assay Bos taurus L-glutamate + H2O + NADP+
-
r
L-glutamate + H2O + NAD(P)+
-
Bos taurus 2-oxoglutarate + NH3 + NAD(P)H
-
r

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0065
-
GTP 1 mM NAD+ or 80 mM NADH Bos taurus
0.009
-
GTP 0.08 mM NADH Bos taurus
0.012
-
GTP 0.016 mM NADH Bos taurus
0.018
-
GTP 1 mM NADP+ Bos taurus