The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain.
The complexation of ribulosebiphosphate carboxylase with CO2, Mg2+, and carboxyarabinitol bisphosphate (CABP) to produce the quaternary enzyme-carbamate-Mg2+-CABP complex closely mimics the formation of the catalytically competent enzyme-carbamate-Mg2+-3-keto-CABP form during enzymatic catalysis. Quaternary complexes were prepared with various metals (Mg2+, Cd2+, Mn2+, Co2+, and Ni2+) and with specifically 13C-enriched ligands. 31P and 13C NMR studies of these complexes demonstrate that the activator CO2 site (carbamate site), the metal binding site, and the substrate binding site are contiguous. It follows that both the carboxylase and oxygenase activities of this bifunctional enzyme are influenced by the structures of the catalytic and activation sites.
Pierce
J
J
Reddy
G S
GS
D001665:Binding Sites; D002245:Carbon Dioxide / Q000378:metabolism; D002384:Catalysis; D002413:Cations, Divalent / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004789:Enzyme Activation; D009682:Magnetic Resonance Spectroscopy; D008670:Metals / Q000378:metabolism; D010428:Pentosephosphates / Q000138:chemical synthesis / Q000378:metabolism; D011485:Protein Binding; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013402:Sugar Alcohols
D002413:Cations, Divalent; D008670:Metals; D010428:Pentosephosphates; D013402:Sugar Alcohols; D002245:Carbon Dioxide; C032687:2-carboxyarabinitol 1,5-biphosphate; D012273:Ribulose-Bisphosphate Carboxylase