Bryophyllum fedtschenkoi protein phosphatase type 2A can dephosphorylate phosphoenolpyruvate carboxylase

Carter, P.J., Nimmo, H.G. , Fewson, C.A. and Wilkins, M.B. (1990) Bryophyllum fedtschenkoi protein phosphatase type 2A can dephosphorylate phosphoenolpyruvate carboxylase. FEBS Letters, 263(2), pp. 233-236. (doi: 10.1016/0014-5793(90)81381-W)

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Abstract

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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Carter, P.J., Nimmo, H.G., Fewson, C.A., and Wilkins, M.B.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:FEBS Letters
Publisher:Elsevier Science Publishers
ISSN:0014-5793
ISSN (Online):1873-3468

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