The Enzyme Database

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Accepted name: [pyruvate, phosphate dikinase]-phosphate phosphotransferase
Reaction: [pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate
Other name(s): PPDK regulatory protein (ambiguous); pyruvate, phosphate dikinase regulatory protein (ambiguous); bifunctional dikinase regulatory protein (ambiguous); PDRP1 (gene name)
Systematic name: [pyruvate, phosphate dikinase]-phosphate:phosphate phosphotransferase
Comments: The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate, phosphate dikinase (EC, cf. EC, [pyruvate, phosphate dikinase] kinase [2-5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 231 (1984) 175–182. [DOI] [PMID: 6326674]
2.  Burnell, J.N. and Hatch, M.D. Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase. Arch. Biochem. Biophys. 237 (1985) 490–503. [DOI] [PMID: 2983615]
3.  Chastain, C.J., Botschner, M., Harrington, G.E., Thompson, B.J., Mills, S.E., Sarath, G. and Chollet, R. Further analysis of maize C4 pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues. Arch. Biochem. Biophys. 375 (2000) 165–170. [DOI] [PMID: 10683263]
4.  Burnell, J.N. and Chastain, C.J. Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene. Biochem. Biophys. Res. Commun. 345 (2006) 675–680. [DOI] [PMID: 16696949]
5.  Chastain, C.J., Xu, W., Parsley, K., Sarath, G., Hibberd, J.M. and Chollet, R. The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure. Plant J. 53 (2008) 854–863. [DOI] [PMID: 17996018]
[EC created 2012]

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