Abstract
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.
MeSH Terms
Adenosine Triphosphate
Animals
Bicarbonates
Cattle
Glutamates
Kinetics
Liver/enzymology
Magnesium
Models, Chemical
Phosphotransferases/metabolism
Quaternary Ammonium Compounds
Chemicals
Bicarbonates
Glutamates
Quaternary Ammonium Compounds
Adenosine Triphosphate
Phosphotransferases
Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Elliott K R
Tipton K F
References (13)
13 references, click to expand
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