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. 1973 May;134(1):209–215. doi: 10.1042/bj1340209

Effect of l-leucine on the nitrogen metabolism of isolated rat liver mitochondria

J D McGivan 1, Norah M Bradford 1, M Crompton 1, J B Chappell 1
PMCID: PMC1177801  PMID: 4723223

Abstract

1. l-Leucine strongly activated intramitochondrial glutamate dehydrogenase in the direction of glutamate synthesis. 2. In the deamination direction, the enzyme was not stimulated by leucine. This was probably due to a rate-limiting transport of glutamate across the mitochondrial membrane. 3. The effect of leucine on the kinetic constants of glutamate dehydrogenase in a mitochondrial sonicate was studied. 4. In isolated mitochondria, leucine did not stimulate the synthesis of citrulline with glutamate as the source of NH3. 5. Leucine very markedly stimulated the synthesis of glutamate from added 2-oxoglutarate+NH4Cl. 6. Under conditions where glutamate and citrulline could be synthesized simultaneously from added NH4Cl, leucine greatly increased glutamate synthesis at the expense of citrulline synthesis. 7. It is suggested that the intramitochondrial leucine concentration may be a factor influencing the nitrogen metabolism of the liver cell.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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