Cloned (Comment) | Organism |
---|---|
recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL | Zea mays |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Zea mays | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
[pyruvate, phosphate dikinase] phosphate + phosphate | Zea mays | - |
[pyruvate, phosphate dikinase] + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | Q195N6 | gene PDRP1 | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography | Zea mays |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[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 |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
[pyruvate, phosphate dikinase] phosphate + phosphate | - |
Zea mays | [pyruvate, phosphate dikinase] + diphosphate | - |
? | |
[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 | ? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
PDRP | - |
Zea mays |
PDRP1 | - |
Zea mays |
PPDK regulatory protein | - |
Zea mays |
pyruvate orthophosphate dikinase regulatory protein | - |
Zea mays |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
asay at | Zea mays |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
dephosphorylation assay at | Zea mays |
8.3 | - |
kinase assay at | Zea mays |
General Information | Comment | Organism |
---|---|---|
evolution | PDRP shares no significant sequence similarity with other protein kinases or phosphatases | Zea mays |
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 |
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 |