Al. Twerdochlib et al., L-RHAMNOSE METABOLISM IN PICHIA-STIPITIS AND DEBARYOMYCES-POLYMORPHUS, Canadian journal of microbiology, 40(11), 1994, pp. 896-902
The pathway for the breakdown of L-rhamnose by the yeast Pichia stipit
is NRC 5568 was shown to involve nonphosphorylated intermediates and t
o produce pyruvate and L-lactaldehyde. The activities of the enzymes a
nd the nature of several intermediates were determined. The enzymes in
volved are L-rhamnose dehydrogenase, L-rhamnonate dehydratase, and 2-k
eto-3-deoxy-L-rhamnonate aldolase. This pathway was found to be induci
ble by L-rhamnose and repressed by D-glucose. These enzymes were also
present in a mutant of P. stipitis (PR1) resistant to catabolite repre
ssion and in Debaryomyces polymorphus 1747. Cell-free extracts of P. s
tipitis and D. polymorphus grown in L-rhamnose as sole carbon source w
ere found to contain NAD(+)-dependent aldehyde dehydrogenase activitie
s.