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Literature summary extracted from

  • Chastain, C.J.; Chollet, R.
    Regulation of pyruvate, orthophosphate dikinase by ADP-/Pi-dependent reversible phosphorylation in C3 and C4 plants (2003), Plant Physiol. Biochem., 41, 523-532.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.32
-
 Zea mays

Protein Variants

EC Number Protein Variants Comment Organism
2.7.9.1 H458N no activity Zea mays
2.7.9.1 T456D no activity Zea mays
2.7.9.1 T456E no activity Zea mays
2.7.9.1 T456F 1% activity with respect to wild type Zea mays
2.7.9.1 T456S 111% activity with respect to wild type Zea mays
2.7.9.1 T456V 98% activity with respect to wild type Zea mays
2.7.9.1 T456Y 6% activity with respect to wild type Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.32 pyruvate likely inhibits the threonyl-phosphorylation of pyruvate, orthophosphate dikinase by direct competition with regulatory protein for the requisite E-HisP reaction intermediate during catalysis by pyruvate, orthophosphate dikinase, pH not specified in the publication, temperature not specified in the publication Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.32 0.0012
-
 pyruvate, phosphate dikinase pH not specified in the publication, temperature not specified in the publication Zea mays
2.7.11.32 0.05
-
 ADP pH not specified in the publication, temperature not specified in the publication Zea mays

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.9.1 95000
-
 4 * 95000, dissociates into largely inactive dimers and tetramers when subjected to cold temperatures in vitro Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate Zea mays activity strictly and reversibly regulated by light AMP + phosphoenolpyruvate + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 Zea mays
-
-
-
2.7.11.32 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.32
-
 Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.9.1 mesophyll
-
 Zea mays
-
2.7.11.32 leaf
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate
-
 Zea mays AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.1 ATP + pyruvate + phosphate activity strictly and reversibly regulated by light Zea mays AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.11.32 pyruvate, phosphate dikinase + ADP His458 phosphorylated, active Zea mays [pyruvate, phosphate dikinase] phosphate + AMP His458 and Thr456 phosphorylated (inactive), T456S mutant protein substrate is also phosphorylated, H456N mutant protein substrat is not phosphorylated ?

Subunits

EC Number Subunits Comment Organism
2.7.9.1 tetramer 4 * 95000, dissociates into largely inactive dimers and tetramers when subjected to cold temperatures in vitro Zea mays
2.7.11.32 More additional information from earlier studies included (a) estimates of a monomeric molecular mass of 45000-48000, as determined by size exclusion chromatography and one-dimensional SDS-PAGE; (b) pH-dependent changes in aggregation state (dimeric at pH 7.5, tetrameric at pH 8.3) Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.7.11.32 PPDK regulatory protein
-
 Zea mays
2.7.11.32 pyruvate, orthophosphate dikinase regulatory protein bifunctional protein kinase/phosphatase Zea mays

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.32 0.08
-
 pyruvate likely inhibits the threonyl-phosphorylation of pyruvate, orthophosphate dikinase by direct competition with regulatory protein for the requisite E-HisP reaction intermediate during catalysis by pyruvate, orthophosphate dikinase, pH not specified in the publication, temperature not specified in the publication Zea mays