Catabolite inactivation, cyclic AMP and protein phosphorylation in the methylotrophic yeast Hansenula polymorpha

Antonie Van Leeuwenhoek. 1991 Jul;60(1):49-54. doi: 10.1007/BF00580441.

Abstract

The inactivation of the peroxisomal enzyme alcohol oxidase and the cytoplasmic enzymes fructose-1,6-bisphosphatase, malate dehydrogenase and phosphoenolpyruvate carboxykinase was found to occur after addition of glucose to methanol-grown cells of the yeast Hansenula polymorpha. The concentration of cyclic AMP increased nearly twofold within 3 min under the same conditions. In crude extracts of H. polymorpha about 20 proteins are phosphorylated by cyclic AMP dependent protein kinases, among them also fructose-1,6-bisphosphatase. No phosphorylation of the alcohol oxidase protein could be detected. From this fact, it was concluded that the inactivation of the peroxisomal alcohol oxidase is independent of cyclic AMP-dependent protein phosphorylation.

MeSH terms

  • Alcohol Oxidoreductases / antagonists & inhibitors
  • Alcohol Oxidoreductases / metabolism
  • Cyclic AMP / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Fructose-Bisphosphatase / metabolism*
  • Fungal Proteins / metabolism*
  • Malate Dehydrogenase / antagonists & inhibitors
  • Malate Dehydrogenase / metabolism
  • Methanol / metabolism
  • NADP / metabolism*
  • Phosphoenolpyruvate Carboxykinase (GTP) / metabolism*
  • Phosphorylation
  • Pichia / enzymology
  • Pichia / metabolism*
  • Protein Kinases / metabolism
  • Staining and Labeling

Substances

  • Fungal Proteins
  • NADP
  • Cyclic AMP
  • Alcohol Oxidoreductases
  • Malate Dehydrogenase
  • alcohol oxidase
  • Protein Kinases
  • Fructose-Bisphosphatase
  • Phosphoenolpyruvate Carboxykinase (GTP)
  • Methanol