ExplorEnz: EC 2.7.4.27

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2.7.4.27

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 2.7.9.1), cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase [2-5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

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,P_i 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 P_i-mediated activation of pyruvate,P_i 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, P_i 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 2.7.4.27 created 2012]