[Activity of pentose phosphate pathway enzymes in alkane-oxidizing yeast cells].
The activity of the key enzymes of the pentose phosphate pathway (glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, transketolase) was determined in cell-free homogenates of Candida lipolytica 695 and Candida tropicalis 303 growing on different carbon sources. The activity of these enzymes remained almost the same in the course of growth of both cultures. The activity of the enzymes differed only slightly in the cells metabolizing hexadecane and glucose. The activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the cell-free homogenates of C. tropicalis 303 was twice as high as in the cells of C. lipolytica 695. The activity of transketolase was the same in both cultures. The main role of the pentose phosphate pathway is presumed to consist not in catabolism of the carbon source, but in biosynthesis of pentoses and other important intermediates.
D000473:Alkanes / Q000378:metabolism*; D002175:Candida / Q000201:enzymology*; D002474:Cell-Free System; D003470:Culture Media; D005947:Glucose / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D010734:Phosphogluconate Dehydrogenase / Q000378:metabolism*; D014174:Transketolase / Q000378:metabolism*
D000473:Alkanes; D003470:Culture Media; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D014174:Transketolase; D005947:Glucose
Aktivnost' fermentov pentozofosfatnogo tsikla v kletkakh alkanokisliaiushchikh drozhzheĭ