Synonyms: L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating); Glutamate Dehydrogenase from bovine liver
CAS Number: 2604152
MDL No.: MFCD00131461
Storage: 2-8C
Enzyme Commission (EC) Number: 1.4.1.3 ( BRENDA | IUBMB )
UNSPSC Code: 12352204
Application: L-glutamic dehydrogenase was used to catalyze the conversion of isocitrate into α-ketoglutarate and carbon dioxide.
Biochem/physiol Actions: Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. The bovine enzyme is characterized by three sets of properties: . It has a reversible concentration-dependent association, producing higher molecular weight forms.. Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.. Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
Physical form: Solution in 50% glycerol, pH 7.3
Unit Definition: One unit will reduce 1.0 mumole of alpha-ketoglutarate to L-glutamate per min at pH 7.3 at 25 C, in the presence of ammonium ions.
Analysis Note: Protein determined by biuret.
RIDADR: NONH for all modes of transport
WGK Germany: 1