Acetyl-coenzyme A carboxylase from the developing endosperm of Ricinus communis. II. A two-site kinetic mechanism.
The reaction kinetics of acetyl-coenzyme A carboxylase purified from developing castor oil seeds have been examined. On the basis of the substrate interaction and product inhibition results, a hybrid ping-pong mechanism is proposed. This type of mechanism demands that the active site of the enzyme be separated into two functionally distinct catalytic sites. The carboxybiotin intermediate formed at one site by the hydrolysis of ATP swings to the second site where acetyl-CoA is carboxylated to form malonyl-CoA. This hybrid rapid-equilibrium random bi bi uni uni ping-pong mechanism which includes the formation of three abortive complexes, E . HCO-3 . ADP, E . HCO-3 . Pi and E . Pi . Pi, is analogous to the hybrid ping-pong mechanism previously described for methylmalonyl-CoA transcarboxylase.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D001665:Binding Sites; D001667:Binding, Competitive; D001710:Biotin / Q000494:pharmacology; D002367:Ricinus communis / Q000201:enzymology*; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008433:Mathematics; D010947:Plants, Toxic; D011485:Protein Binding; D012278:Ricinus / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology*
D001710:Biotin; D008025:Ligases; D000103:Acetyl-CoA Carboxylase