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J Biol Chem, Vol. 273, Issue 40, 25751-25756, October 2, 1998

An Investigation of the Metabolism of Valine to Isobutyl Alcohol in Saccharomyces cerevisiae

J. Richard Dickinson, Scott J. Harrison^¶, and Michael J. E. Hewlins

From the  School of Pure & Applied Biology, University of Wales, Cardiff, CF1 3TL, the ^¶ MassLab Group, Finnigan PLC, Wythenshawe, Manchester, M23 9BE, and the  Department of Chemistry, University of Wales, Cardiff, CF1 3TB, United Kingdom

The metabolism of valine to isobutyl alcohol in yeast was examined by ¹³C nuclear magnetic resonance spectroscopy and combined gas chromatography-mass spectrometry. The product of valine transamination, -ketoisovalerate, had four potential routes to isobutyl alcohol. The first, via branched-chain -ketoacid dehydrogenase to isobutyryl-CoA is not required for the synthesis of isobutyl alcohol because abolition of branched-chain -ketoacid dehydrogenase activity in an lpd1 disruption mutant did not prevent the formation of isobutyl alcohol. The second route, via pyruvate decarboxylase, is the one that is used because elimination of pyruvate decarboxylase activity in a pdc1 pdc5 pdc6 triple mutant virtually abolished isobutyl alcohol production. A third potential route involved -ketoisovalerate reductase, but this had no role in the formation of isobutyl alcohol from -hydroxyisovalerate because cell homogenates could not convert -hydroxyisovalerate to isobutyl alcohol. The final possibility, use of the pyruvate decarboxylase-like enzyme encoded by YDL080c, seemed to be irrelevant, because a strain with a disruption in this gene produced wild-type levels of isobutyl alcohol. Thus there are major differences in the catabolism of leucine and valine to their respective "fusel" alcohols. Whereas in the catabolism of leucine to isoamyl alcohol the major route is via the decarboxylase encoded by YDL080c, any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine. Finally, analysis of the ¹³C-labeled products revealed that the pathways of valine catabolism and leucine biosynthesis share a common pool of -ketoisovalerate.

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