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- W2092912383 abstract "Although heart mitochondria contain glutamate dehydrogenase, it has not been thought to play a role in their metabolism. We investigated this matter to define the conditions under which it is active. We found modest activity in the presence of glutamate and malate and a continuous source of ADP when pyruvate is added. This increases several fold as the osmolarity is increased from 296 to 370 moSM. At the higher osmolarity ammonia formation is brief, associated with a lower intramitochondrial α-ketoglutarate content and a 17% drop in glutamate conversion to α-ketoglutarate. Formation of α-ketoglutarate from citrate does not make up for the drop in glutamate conversion to α-ketoglutarate. Mitochondrial content of nucleotides and CoA compounds are not altered by pyruvate addition. The rate of glutamate deamination by GDH in sonicated heart mitochondria agrees with the rate of ammonia formation in intact mitochondria in the presence of pyruvale (20 nmol/min/mg of mitochondrial protein). We conclude pyruvate lowers mitochondrial oxalacetate which decreases α-ketoglutarate formation by transamination. The lower mitochondria α-ketoglutarate level permits glutamate deamination until α-ketoglutarate reaches a level that inhibits the forward reaction. Further proof of the key role of α-ketoglutarate is seen with aminooxyacetate which blocks transamination. In its presence ammonia formation occurs at the same rate (18 nm/min/mg of mitochondrial protein), is not dependent upon pyruvate, and does not stop after a couple of minutes. Leucine, which decreases α-ketoglutarate inhibition of GDH, also results in ammonia formation, further supporting the concept of regulation by α-ketoglutarate. The higher osmolarity increases GDH activity by increasing α-ketoglutarate transport from mitochondria." @default.
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- W2092912383 date "1993-08-01" @default.
- W2092912383 modified "2023-09-25" @default.
- W2092912383 title "Conditions for Glutamate Dehydrogenase Activity in Heart Mitochondria" @default.
- W2092912383 doi "https://doi.org/10.1006/bmmb.1993.1048" @default.
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