Irreversible inactivation of Saccharomyces cerevisiae fructose-1,6-bisphosphatase independent of protein phosphorylation at Ser11

Matthias Rose, Karl Dieter Entian, Lucia Hofmann, Rudi F. Vogel, Dieter Mecke

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The fructose-1,6-bisphosphatase gene was used with multicopy plasmids to study rapid reversible and irreversible inactivation after addition of glucose to derepressed Saccharomyces cerevisiae cells. Both inactivation systems could inactivate the enzyme, even if 20-fold over-expressed. The putative serine residue, at which fructose-1,6-bisphosphatase is phosphorylated, was changed to an alanine residue without notably affecting the catalytic activity. No rapid reversible inactivation was observed with the mutated enzyme. Nonetheless, the modified enzyme was still irreversibly inactivated, clearly demonstrating that phosphorylation is an independent regulatory circuit that reduces fructose-1,6-bisphosphatase activity within seconds. Furthermore, irreversible glucose inactivation was not triggered by phosphorylation of the enzyme.

Original languageEnglish
Pages (from-to)55-59
Number of pages5
JournalFEBS Letters
Volume241
Issue number1-2
DOIs
StatePublished - 5 Dec 1988
Externally publishedYes

Keywords

  • (Saccharomyces cerevisiae)
  • Carbohydrate metabolism
  • Fructose-1,6-bisphosphatase
  • Irreversible inactivation
  • Phosphorylation
  • Reversible inactivation

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