Sucrose‐phosphate synthase phosphatase, a type 2A protein phosphatase, changes its sensitivity towards inhibition by inorganic phosphate in spinach leaves

FEBS Letters

Weiner, Heike¹  Weiner, Hendrik¹  Stitt, Mark¹ 

[1] Botanisches Institut der Universität Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany

关键词: SPS-P;    sucrose-phosphate synthase phosphatase;    Pi;    inorganic phosphate;    MOPS;    3-(N-morpholino)propane sulfonic acid;    ATP;    adenosine 5-triphosphate;    CHX;    cycloheximide;    BSA;    bovine serum albumin;    Protein phosphatase 2A;    Sucrose-phosphate synthase;    Phosphate inhibition;    Protein phosphorylation;    Light and mannose activation;   

DOI  :  10.1016/0014-5793(93)80396-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The activity of a type 2A protein phosphatase from spinach leaves was monitored using phosphorylated sucrose-phosphate synthase (SPS) as a substrate. After partial purification the overall activities of sucrose-phosphate synthase phosphatase (SPS-P) recovered from leaves harvested in the dark and in the light did not vary. However, SPS-P preparations from darkened leaves were more strongly inhibited by inorganic phosphate and certain phosphorylated compounds than preparations from illuminated or mannose fed leaves. We conclude, that activation of SPS involves an interconversion of multiple forms of SPS-P activity.

【 授权许可】

Unknown