Degradation of microbodies in relation to activities of alcohol oxidase and catalase in Candida boidinii.
Degradation of microbodies in the methanol-utilizing yeast Candida boidinii was mainly studied by electron microscopical observation. The yeast cells precultured on methanol medium contained five to six  microbodies per section and showed high activities of alcohol oxidase, catalase, formaldehyde dehydrogenase and formate dehydrogenase. When the precultured cells were transferred into an ethanol medium the number of microbodies and concomitantly the activities of alcohol oxidase and catalase decreased. After 6 h of cultivation microbodies were hardly detected. Also the activity of alcohol oxidase was not measurable and catalase activity was reduced to one tenth, whereas the activities of formaldehyde dehydrogenase and formate dehydrogenase decreased only to about 70%. Experiments with methanol-grown cells transferred into an ethanol medium without nitrogen source indicated that the inactivation of alcohol oxidase and catalase does not require protein synthesis. However, the reappearance of these enzymes is presumably due to de novo protein synthesis as shown by experiments with cycloheximide.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D002175:Candida / Q000201:enzymology / Q000378:metabolism / Q000648:ultrastructure*; D002374:Catalase / Q000378:metabolism*; D003513:Cycloheximide / Q000494:pharmacology; D000431:Ethanol / Q000378:metabolism; D000432:Methanol / Q000378:metabolism; D008830:Microbodies / Q000648:ultrastructure
D000431:Ethanol; D003513:Cycloheximide; D000429:Alcohol Oxidoreductases; D002374:Catalase; D000445:Aldehyde Oxidoreductases; D000432:Methanol