Kinetic studies of bovine liver carbamoyl phosphate synthetase.
A through study of initial-rate data has been made on carbamoyl phosphate synthetase from bovine liver. On the basis of the results the order of substrate binding to the enzyme is ATPMg followed by HCO(3) (-), ATPMg and NH(4) (+). A model for the enzymic mechanism is proposed, and the rate equations describing it are presented. Details of the derivation of the initial-rate equation for the kinetic mechanism proposed have been deposited as Supplementary Publication SUP 50032 (6 pages) at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7QB, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1973), 131, 5.
D000255:Adenosine Triphosphate; D000818:Animals; D001639:Bicarbonates; D002417:Cattle; D005971:Glutamates; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium; D008956:Models, Chemical; D010770:Phosphotransferases / Q000378:metabolism*; D000644:Quaternary Ammonium Compounds
D001639:Bicarbonates; D005971:Glutamates; D000644:Quaternary Ammonium Compounds; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D008274:Magnesium