BRYOPHYLLUM-FEDTSCHENKOI PROTEIN PHOSPHATASE TYPE-2A CAN DEPHOSPHORYLATE PHOSPHOENOLPYRUVATE CARBOXYLASE

被引：95

作者：

CARTER, PJ

NIMMO, HG

FEWSON, CA

WILKINS, MB

机构：

[1] UNIV GLASGOW,DEPT BIOCHEM,GLASGOW G12 8QQ,SCOTLAND

[2] UNIV GLASGOW,DEPT BOT,GLASGOW G12 8QQ,SCOTLAND

来源：

FEBS LETTERS | 1990年 / 263卷 / 02期

关键词：

(Bryophyllum fedtschenkoi); Crassulacean acid metabolism; Malate inhibition; Phosphoenolpyruvate carboxylase; Phosphorylation; Protein phosphatase;

D O I：

10.1016/0014-5793(90)81381-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphoenolpyruvate carboxylase, which catalyses the nocturnal fixation of CO2 in Crassulacean acid metabolism (CAM) plants, is regulated by reversible phosphorylation. The phosphorylated 'night' form of the enzyme is ten-fold less sensitive to inhibition by malate than is the dephosphorylated 'day' form. The phosphoenolpyruvate carboxylase of the CAM plant Bryophyllum fedtschenkoi can be dephosphorylated by rabbit muscle protein phosphatase type 2A but not by type 1. B. fedtschenkoi leaves contain protein phosphatase activity that can dephosphorylate phosphoenolpyruvate carboxylase. Inhibitor studies show that this enzyme is a type 2A protein phosphatase. © 1990.

引用

页码：233 / 236

页数：4

共 15 条

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MCGOWAN CH, 1988, METHOD ENZYMOL, V159, P416

[12] PERSISTENT CIRCADIAN-RHYTHMS IN THE PHOSPHORYLATION STATE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM BRYOPHYLLUM-FEDTSCHENKOI LEAVES AND IN ITS SENSITIVITY TO INHIBITION BY MALATE [J].