Induction of N-acetylglucosamine-catabolic pathway in spheroplasts of Candida albicans.
Synthesis of N-acetylglucosamine-catabolic enzymes, namely permease (high-affinity uptake system), kinase and deaminase was studied in the spheroplasts of the yeast Candida albicans. The presence of N-acetylglucosamine as inducer is essential for the induced synthesis of these enzymes in the spheroplasts, which were active for at least 8--9 h. However, some of the newly synthesized kinase and deaminase leaked out from the spheroplasts into the medium during induction. Experiments with inhibitors of RNA and protein synthesis indicate that the appearance of new enzyme activities is dependent on concomitant new protein synthesis and the inducer operates at a transcriptional level. However, inhibitors of DNA synthesis, e.g. mitomycin-C and hydroxyurea, had no effect on the synthesis of these enzymes.
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000378:metabolism*; D000581:Amidohydrolases / Q000096:biosynthesis; D002176:Candida albicans / Q000201:enzymology*; D002238:Carbohydrate Epimerases / Q000096:biosynthesis; D004790:Enzyme Induction; D005944:Glucosamine / Q000031:analogs & derivatives*; D005958:Glucosephosphates; D046911:Macromolecular Substances; D010770:Phosphotransferases / Q000096:biosynthesis; D013104:Spheroplasts / Q000201:enzymology*
D005958:Glucosephosphates; D046911:Macromolecular Substances; D010770:Phosphotransferases; D000581:Amidohydrolases; D002238:Carbohydrate Epimerases; D005944:Glucosamine; D000117:Acetylglucosamine