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Literature summary extracted from

  • Jiang, L.; Chen, Y.B.; Zheng, J.; Chen, Z.; Liu, Y.; Tao, Y.; Wu, W.; Chen, Z.; Wang, B.C.
    Structural basis of reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein (2016), Plant Physiol., 170, 732-741.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.27 recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL Zea mays

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.27 purified apoenzyme, mixing of 10 mg/m protein with a well solution containing 1.0 M K/Na tartrate, 0.1 M MOPS, pH 8.0, 1% dioxane, 1 mM AMP, and 2 mM Mg2+,.X-ray diffraction structure determination and analysis at 3.2 A resolution Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.27 chloroplast
-
 Zea mays 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.27 Mg2+ required Zea mays
2.7.9.1 Mg2+ required Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.27 additional information Zea mays pyruvate orthophosphate dikinase regulatory protein, PDRP, is a bifunctional enzyme that catalyzes both phosphorylation and dephosphorylation of the pyruvate orthophosphate dikinase. Enzyme PDRP uses ADP as the phosphoryl donor for kinase activity, and employs a phosphate-dependent, diphosphate-forming dephosphorylation mechanism ?
-
 ?
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate Zea mays
-
 [pyruvate, phosphate dikinase] + diphosphate
-
 ?
2.7.9.1 ATP + pyruvate + phosphate Zea mays
-
 AMP + phosphoenolpyruvate + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.27 Zea mays Q195N6 gene PDRP1
-
2.7.9.1 Zea mays
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.9.1 phosphoprotein reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein (PDRP) , structural analysis and molecular catalytic mechanism, overview. The homodimeric PPDK regulatory protein regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation. Residue Asp277 is used for protonating and deprotonating the target Thr residue of PPDK to promote nucleophilic attack Zea mays

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.27 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography Zea mays

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate enzyme PDRP contains a single active site that catalyzes both phosphorylation and dephosphorylation, cf. EC 2.7.11.32. Catalytic mechanism of PPDK regulatory protein, overview Zea mays
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.27 leaf
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.27 additional information pyruvate orthophosphate dikinase regulatory protein, PDRP, is a bifunctional enzyme that catalyzes both phosphorylation and dephosphorylation of the pyruvate orthophosphate dikinase. Enzyme PDRP uses ADP as the phosphoryl donor for kinase activity, and employs a phosphate-dependent, diphosphate-forming dephosphorylation mechanism Zea mays ?
-
 ?
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate
-
 Zea mays [pyruvate, phosphate dikinase] + diphosphate
-
 ?
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate
-
 Zea mays [pyruvate, phosphate dikinase] + diphosphate reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27 ?
2.7.9.1 ATP + pyruvate + phosphate
-
 Zea mays AMP + phosphoenolpyruvate + diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.4.27 homodimer enzyme PDRP forms a compact homodimer in which each protomer contains two separate N-terminal and C-terminal domains. The N-terminal domain has conserved intramolecular and intermolecular disulfide bonds for enzyme PDRP dimerization. Three-dimensional structure analysis, overview. The C-terminal domain is the site of both kinase and diphosphorylase activities Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.7.4.27 PDRP
-
 Zea mays
2.7.4.27 PDRP1
-
 Zea mays
2.7.4.27 PPDK regulatory protein
-
 Zea mays
2.7.4.27 pyruvate orthophosphate dikinase regulatory protein
-
 Zea mays
2.7.9.1 PPDK
-
 Zea mays
2.7.9.1 pyruvate orthophosphate dikinase
-
 Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.27 30
-
 asay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.27 8
-
 dephosphorylation assay at Zea mays
2.7.4.27 8.3
-
 kinase assay at Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.9.1 AMP
-
 Zea mays
2.7.9.1 ATP
-
 Zea mays

General Information

EC Number General Information Comment Organism
2.7.4.27 evolution PDRP shares no significant sequence similarity with other protein kinases or phosphatases Zea mays
2.7.4.27 additional information PDRP forms a compact homodimer in which each protomer contains two separate N-terminal and C-terminal domains. The C-terminal domain includes several key elements for performing both phosphorylation and dephosphorylation activities: the phosphate binding loop (P-loop) for binding the ADP and inorganic phosphate substrates, residues Lys274 and Lys299 for neutralizing the negative charge, and residue Asp277 for protonating and deprotonating the target Thr residue of PPDK to promote nucleophilic attack. The N-terminal domain shares the same protein fold as the C-terminal domain and also includes a putative P-loop with AMP bound but lacking enzymatic activities. This loop may participate in the interaction with and regulation of enzyme PPDK. The N-terminal domain has conserved intramolecular and intermolecular disulfide bonds for PDRP dimerization. Three-dimensional structure analysis, overview Zea mays
2.7.4.27 physiological function PPDK regulatory protein (PDRP) regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation. Pyruvate orthophosphate dikinase (PPDK) is one of the most important enzymes in C4 photosynthesis Zea mays
2.7.9.1 physiological function PPDK regulatory protein (PDRP) regulates the phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation Zea mays