Pyruvate carboxylase from chicken liver. Steady state kinetic studies indicate a "two-site" ping-pong mechanism.
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000494:Allosteric Regulation; D000818:Animals; D001639:Bicarbonates; D001665:Binding Sites; D001710:Biotin; D002245:Carbon Dioxide; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003065:Coenzyme A; D003653:Decarboxylation; D005246:Feedback; D007700:Kinetics; D008025:Ligases; D008099:Liver / Q000201:enzymology*; D008274:Magnesium; D008314:Malonates; D008433:Mathematics; D008956:Models, Chemical; D010071:Oxaloacetates; D010710:Phosphates; D011773:Pyruvates; D014166:Transferases
D001639:Bicarbonates; D008314:Malonates; D010071:Oxaloacetates; D010710:Phosphates; D011773:Pyruvates; D002245:Carbon Dioxide; D000249:Adenosine Monophosphate; D001710:Biotin; D000255:Adenosine Triphosphate; D014166:Transferases; D008025:Ligases; D008274:Magnesium; D003065:Coenzyme A