Product inhibition studies on bovine liver carbamoyl phosphate synthetase.
A study of the product-inhibition patterns of carbamoyl phosphate synthetase from bovine liver is reported. Inhibition by adenosine, AMP and inorganic ions is also reported. The results are in agreement with the previously proposed model in which the order of substrate binding is ATPMg, followed by HCO(3) (-), ATPMg and NH(4) (+). The order of product release on the basis of the reported results is carbamoyl phosphate, followed by ADPMg, ADPMg and inorganic phosphate.
D000241:Adenosine / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate; D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology; D002219:Carbamates; D002417:Cattle; D005246:Feedback; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D011188:Potassium / Q000494:pharmacology; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology
D001639:Bicarbonates; D002219:Carbamates; D000644:Quaternary Ammonium Compounds; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D008274:Magnesium; D000241:Adenosine; D011188:Potassium