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The pathway for the breakdown of L-rhamnose by the yeast Pichia stipitis NRC 5568 was shown to involve nonphosphorylated intermediates and to produce pyruvate and L-lactaldehyde. The activities of the enzymes and the nature of several intermediates were determined. The enzymes involved are L-rhamnose dehydrogenase, L-rhamnonate dehydratase, and 2-keto-3-deoxy-L-rhamnonate aldolase. This pathway was found to be inducible by L-rhamnose and repressed by D-glucose. These enzymes were also present in a mutant of P. stipitis (PR1) resistant to catabolite repression and in Debaryomyces polymorphus 1747. Cell-free extracts of P. stipitis and D. polymorphus grown in L-rhamnose as sole carbon source were found to contain NAD+-dependent aldehyde dehydrogenase activities.
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Twerdochlib et al. (1994) studied this question.
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