publication . Article . 2002

Effects of Phosphorylation on Phosphoenolpyruvate Carboxykinase from the C4 Plant Guinea Grass\ud

Walker, R.P.; Chen, Z.; Acheson, R.M.; Leegood, R.C.;
Open Access English
  • Published: 01 Jan 2002
  • Country: United Kingdom
In the C4 plant Guinea grass (Panicum maximum), phosphoenolpyruvate carboxykinase (PEPCK) is phosphorylated in darkened leaves and dephosphorylated in illuminated leaves. To determine whether the properties of phosphorylated and non-phosphorylated PEPCK were different, PEPCK was purified to homogeneity from both illuminated and darkened leaves. The final step of the purification procedure, gel filtration chromatography, further separated phosphorylated and non-phosphorylated forms. In the presence of a high ratio of ATP to ADP, the non-phosphorylated enzyme had a higher affinity for its substrates, oxaloacetate and phosphoenolpyruvate. The activity of the non-ph...

1 This research was supported by the Biotechnology and Biological Sciences Research Council, UK (research grant nos. CO5229 and RSP07804), by a David Phillips Research Fellowship to R.P.W., by a research studentship to R.M.A.

2 These authors contributed equally to the paper.

* Corresponding author; e-mail; fax 44 -114 -222- 0002.

Article, publication date, and citation information can be found at

Acta Phytophys Sin 20: 353-359 Ray TB, Black CC Jr (1976) Characterization of phosphoenolpyruvate carboxykinase from Panicum maximum.

Planta 195: 58-63 Wingler A, Walker RP, Chen Z-H, Leegood RC (1999) Phosphoenolpyruvate carboxykinase is involved in the decarboxylation of aspartate in the bundle-sheath of maize. Plant Physiol 120: 539-545 Wood HG, Davies JJ, Lochmu¨ ller H (1966) The equilibria of reactions catalyzed by carboxytransphosphorylase, carboxykinase and pyruvate carboxylase and the synthesis of phosphoenolpyruvate. J Biol Chem 241: 5692-5704 [OpenAIRE]

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