Transport and metabolism of D-lactate in Jerusalem artichoke mitochondria

Biochim Biophys Acta. 2005 Jun 1;1708(1):13-22. doi: 10.1016/j.bbabio.2005.03.003. Epub 2005 Mar 31.

Abstract

We report here initial studies on D-lactate metabolism in Jerusalem artichoke. It was found that: 1) D-lactate can be synthesized by Jerusalem artichoke by virtue of the presence of glyoxalase II, the activity of which was measured photometrically in both isolated Jerusalem artichoke mitochondria and cytosolic fraction after the addition of S-D-lactoyl-glutathione. 2) Externally added D-lactate caused oxygen consumption by mitochondria, mitochondrial membrane potential increase and proton release, in processes that were insensitive to rotenone, but inhibited by both antimycin A and cyanide. 3) D-lactate was metabolized inside mitochondria by a flavoprotein, a putative D-lactate dehydrogenase, the activity of which could be measured photometrically in mitochondria treated with Triton X-100. 4) Jerusalem artichoke mitochondria can take up externally added D-lactate by means of a D-lactate/H(+) symporter investigated by measuring the rate of reduction of endogenous flavins. The action of the d-lactate translocator and of the mitochondrial D-lactate dehydrogenase could be responsible for the subsequent metabolism of d-lactate formed from methylglyoxal in the cytosol of Jerusalem artichoke.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • Cytosol / enzymology
  • Helianthus / cytology
  • Helianthus / metabolism*
  • Lactate Dehydrogenases / metabolism
  • Lactic Acid / metabolism*
  • Mitochondria / enzymology
  • Mitochondria / metabolism
  • Oxygen Consumption
  • Plant Roots / cytology
  • Plant Roots / enzymology
  • Pyruvaldehyde / metabolism
  • Stereoisomerism
  • Symporters / metabolism
  • Thiolester Hydrolases / metabolism

Substances

  • Symporters
  • Lactic Acid
  • Pyruvaldehyde
  • Lactate Dehydrogenases
  • D-lactate dehydrogenase
  • Thiolester Hydrolases
  • hydroxyacylglutathione hydrolase