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

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

K H Hofmann  1 , E Polnisch
Affiliations

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

K H Hofmann et al. Antonie Van Leeuwenhoek. 1991 Jul.

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.

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