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Literature summary extracted from

  • Erales, J.; Avilan, L.; Lebreton, S.; Gontero, B.
    Exploring CP12 binding proteins revealed aldolase as a new partner for the phosphoribulokinase/glyceraldehyde 3-phosphate dehydrogenase/CP12 complex--purification and kinetic characterization of this enzyme from Chlamydomonas reinhardtii (2008), FEBS J., 275, 1248-1259.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.19 additional information Chlamydomonas reinhardtii association between binding protein CP12 and phosphoribulokinase (EC 2.7.1.19), glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase. The dissociation constant between CP12 and fructose 1,6-bisphosphate (EC 4.1.2.13) aldolase is 0.00048 mM and thus corroborates an interaction between CP12 and aldolase. The dissociation constant between aldolase and the phosphoribulokinase/lyceraldehyde 3-phosphate dehydrogenase/CP12 complex is 55 mM ?
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Organism

EC Number Organism UniProt Comment Textmining
2.7.1.19 Chlamydomonas reinhardtii
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.19 additional information association between binding protein CP12 and phosphoribulokinase (EC 2.7.1.19), glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase. The dissociation constant between CP12 and fructose 1,6-bisphosphate (EC 4.1.2.13) aldolase is 0.00048 mM and thus corroborates an interaction between CP12 and aldolase. The dissociation constant between aldolase and the phosphoribulokinase/lyceraldehyde 3-phosphate dehydrogenase/CP12 complex is 55 mM Chlamydomonas reinhardtii ?
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