Phosphorylation of phosphoenolpyruvate carboxykinase (PEPCK) and phosphoenolpyruvate carboxylase (PEPC) in the flesh of fruits

• Published in: Plant physiology and biochemistry Vol. 108; pp. 323 - 327
• Main Authors: Walker, Robert P., Paoletti, Andrea, Leegood, Richard C., Famiani, Franco
• Format: Journal Article
• Language: English
• Published: France Elsevier Masson SAS 01.11.2016
• Subjects: antiserum; autoradiography; Cucumis sativus - enzymology; Cucumis sativus - metabolism; Developing seeds; Fruit; Fruit - enzymology; Fruit - metabolism; fruits; Gluconeogenesis; grape seeds; grapes; Lycopersicon esculentum - enzymology; Lycopersicon esculentum - metabolism; Magnoliopsida - enzymology; Magnoliopsida - metabolism; Malate; Phosphoenolpyruvate carboxykinase; Phosphoenolpyruvate Carboxykinase (ATP) - metabolism; Phosphoenolpyruvate carboxylase; Phosphoenolpyruvate Carboxylase - metabolism; phosphorus; Phosphorus Radioisotopes - pharmacokinetics; Phosphorylation; Plant Proteins - metabolism; polyacrylamide gel electrophoresis; proteolysis; Prunus - enzymology; Prunus - metabolism; Prunus cerasifera; radionuclides; seeds; Seeds - enzymology; Seeds - growth & development; Tissue Distribution; tomatoes; Vitis - enzymology; Vitis - metabolism; Phosphorylation; Fruit; Malate; Phosphoenolpyruvate carboxykinase; Developing seeds; Phosphoenolpyruvate carboxylase; Gluconeogenesis

This study determined whether phosphoenolpyruvate carboxykinase (PEPCK) and phosphoenolpyruvate carboxylase (PEPC) are phosphorylated in the flesh of a range of fruits. This was done by incubating fruit flesh with 32P[P] (where 32P[P] = 32PO43−), then PEPCK and PEPC were immunoprecipitated from extr...