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

FEBS Letters

Hofmann, Lucia¹  Mecke, Dieter¹  Rose, Matthias¹  Vogel, Rudi F.¹  Entian, Karl-Dieter¹ 

[1]Medizinisch-Naturwissenschaftliches Forschungszentrum, Universität Tübingen, Ob dem Himmelreich 7, D-7400 Tübingen, FRG

关键词: Carbohydrate metabolism;    Fructose-1;    6-bisphosphatase;    Reversible inactivation;    Phosphorylation;    Irreversible inactivation;    (Saccharomyces cerevisiae);    FBPase;    fructose-1;    6-bisphosphatase (EC 3.1.3.11);    FBPaseAla;    mutated FBPase containing alanine instead of serine at position 11;    PEP carboxykinase;    phospho-enolpyruvate carboxykinase (EC 4.1.1.38);    YEP;    yeast extract peptone;    SC;    synthetic complete;   

DOI  :  10.1016/0014-5793(88)81030-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown