منابع مشابه
Kinetic studies on rat liver carbamyl phosphate synthetase.
A partial purification of adult rat liver carbamyl phosphate synthetase is described. The mitochondrial enzyme has been purified to a specific activity of 23.3 pmoles of citrulline per hour per mg of protein. Kinetic studies reveal Michaelis constants for ammonium ion, bicarbonate, ATP, N-acetylglutamic acid, and magnesium similar to the reported values for frog liver carbamyl phosphate synthet...
متن کاملProduct 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 result...
متن کاملCarbamyl phosphate synthetase: studies on the mechanism of action.
The most noteworthy contrasts between the two reactions are the requirement for catalytic amounts of an appropriate derivative of glutamic acid in the case of the liver system, and the difference in stoichiometry with respect to nucleotides. As predicted from thermodynamics the bacterial system is freely reversible; the liver system is not. In this paper, evidence will be presented that the equ...
متن کاملKinetic 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 kine...
متن کاملThe biosynthesis of sucrose phosphate.
The enzymic formation of sucrose from UDPGl and fructose has been described in the preceding paper (1). While some preparations of the enzyme were found to be almost devoid of action of fructose-6-phosphate, other extracts catalyzed the formation of free sucrose either from fructose or from its phosphate. Since these extracts contain phosphatase, it seemed likely that the action on fructose pho...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1978
ISSN: 0014-5793
DOI: 10.1016/0014-5793(78)80576-6