[Control of glutamate dehydrogenase activity in isolated rat liver mitochondria by purine nucleotides, cyclic AMP, alpha-ketoglutarate and phosphate].
Glutamate oxidation by mitochondria in the presence of arsenite and dinitrophenol is diminished by ADP, AMP, GDP and cyclic 3',5'-AMP. Mechanism of inhibition is noncompetitive and atractyloside-sensitive. Alpha-ketoglutarate is a more powerful inhibitor of glutamate oxidation. Inhibitions produced by alpha-ketoglutarate and nucleotide are not additive. Phosphate reverses inhibition of glutamate oxidation produced by nucleotides but only slightly that produced by alpha-ketoglutarate. It is concluded from the results obtained that GDH remains in intact mitochondria under effective control exerted by purine nucleotides (AMP, GDP, ADP, cAMP), alpha-ketoglutarate and phosphate, functioning mainly in the direction of reductive amination of alpha-ketoglutarate.
D000227:Adenine Nucleotides / Q000494:pharmacology*; D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006150:Guanine Nucleotides / Q000494:pharmacology*; D007656:Ketoglutaric Acids / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D010710:Phosphates / Q000494:pharmacology*; D051381:Rats
D000227:Adenine Nucleotides; D006150:Guanine Nucleotides; D007656:Ketoglutaric Acids; D010710:Phosphates; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000242:Cyclic AMP; D005969:Glutamate Dehydrogenase
Reguliatsiia glutamatdegidrogenaznoĭ aktivosti v izolirovannykh mitokhondriiakh pecheni krysy pod vlianiem purinovykh nukleotidov, tsiklicheskogo AMP, AL'FAKETOGLUTARATA I FOSFATA