Biochimica et Biophysica Acta 2008-10-01

Kinetic activation of yeast mitochondrial D-lactate dehydrogenase by carboxylic acids.

Arnaud Mourier, Julie Vallortigara, Edgar D Yoboue, Michel Rigoulet, Anne Devin

Index: Biochim. Biophys. Acta 1777(10) , 1283-8, (2008)

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Abstract

Aerobically grown yeast cells express mitochondrial lactate dehydrogenases that localize to the mitochondrial inner membrane. The D-lactate dehydrogenase is a zinc-flavoprotein with high acceptor specificity for cytochrome c, that catalyzes the oxidation of D-lactate into pyruvate. In this paper, we show that mitochondrial respiratory rate in phosphorylating or non-phosphorylating conditions with D-lactate as substrate is stimulated by carboxylic acids. This stimulation does not affect the yield of oxidative phosphorylation. Furthermore, this stimulation lies at the level of the D-lactate dehydrogenase. It is non-competitive, hyperbolic and its dimension is directly related to the number of carboxylic groups on the activator. The physiological meaning of such a regulation is discussed.

Related Compounds

  • ec 1.1.1.28

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