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Literature summary for 2.7.1.19 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
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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