Ser644 is important for catalytic activity but is not involved in cAMP‐dependent phosphorylation of yeast 6‐phosphofructo‐2‐kinase

FEBS Letters

Keßler, Renate¹  Eschrich, Klaus¹ 

[1] Institute of Biochemistry, University of Leipzig, School of Medicine, Liebigstraße 16, D-04103 Leipzig, Germany

关键词: Glycolysis;    6-Phosphofructo-2-kinase;    Saccharomyces cerevisiae;    Site-directed mutagenesis;   

DOI  :  10.1016/0014-5793(96)01045-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To identify the target amino acid for the cAMP-dependent phosphorylation of yeast 6-phosphofructo-2-kinase Ser⁶⁴⁴ was mutated to Ala. The plasmid-encoded wild-type and mutant enzymes were overexpressed in E. coli TG2 cells and in the yeast strain DFY658. Like the wild-type enzyme, the Ser⁶⁴⁴ → Ala mutant was phosphorylated in vivo after addition of glucose to yeast cells and in vitro by the catalytic subunit of protein kinase A. The specific activity of the mutant enzyme was 6-fold lower than that of the wild-type yeast 6-phosphofructo-2-kinase, but both enzymes were activated in response to the addition of glucose to yeast cells.

【 授权许可】

Unknown