Literature summary for 1.4.1.3 extracted from

Graham, L.D.; Griffin, T.O.; Beatty, R.E.; McCarthy, A.D.; Tipton, K.F.
Purification of liver glutamate dehydrogenase by affinity precipitation and studies on its denaturation (1985), Biochim. Biophys. Acta, 828, 266-269.

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Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-
Rattus norvegicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rattus norvegicus
-	Bos taurus
ammonium sulfate, DEAE-cellulose, affinity precipitation with adipo-N2,N2-dihydrazido-bis(N6-carboxymethyl-NAD+)	Bos taurus

Renatured (Commentary)

Renatured (Comment)	Organism
complete loss of activity after incubation with 6 M guanidine hydrochloride or 7 M urea, no renaturation after dilution into 200 mM phosphate buffer	Rattus norvegicus
complete loss of activity after incubation with 6 M guanidine hydrochloride or 7 M urea, no renaturation after dilution into 200 mM phosphate buffer	Bos taurus

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-
liver	-	Bos taurus	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
37	-	-	Rattus norvegicus
40	-	-	Bos taurus

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)