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Literature summary for 2.7.4.27 extracted from

  • Roeske, C.; Chollet, R.
    Chemical modification of the bifunctional regulatory protein of maize leaf pyruvate,orthophosphate dikinase. Evidence for two distinct active sites (1987), J. Biol. Chem., 262, 12575-12582.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-nitro-5-thiocyanatobenzoate
-
Zea mays
Phenylglyoxal
-
Zea mays
pyridoxal 5'-phosphate
-
Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.67
-
phosphate pH 8.3., 30°C Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
90000
-
90000 at pH 7.5 Zea mays
180000
-
180000 at pH 8.3 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partially purified, ammonium sulfate precipitation, dye ligand chromatography (Blue-Sepharose, agarose-blue dextran), gel filtration Zea mays

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[pyruvate,phosphate dikinase]phosphate + phosphate Thr residue phosphorylated (inactive) Zea mays pyruvate,phosphate dikinase + diphosphate active ir

Subunits

Subunits Comment Organism
homodimer 90000 at pH 7.5 Zea mays
homotetramer 180000 at pH 8.3 Zea mays

Synonyms

Synonyms Comment Organism
bifunctional regulatory protein of pyruvate,orthophosphate dikinase
-
Zea mays

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.7
-
pyridoxal 5'-phosphate pH 8.3, 30°C Zea mays