A kinetic study of hog kidney aminoacylase.
The kinetic and thermodynamic parameters of the hog kidney acylase-catalyzed reactions of N-acetyl-L-methionine hydrolysis and synthesis have been investigated. The equilibrium constants were determined at high concentrations of the products (acetate and L-amino acid) for a number of amino acids. A kinetic scheme of the enzymatic reaction was proposed that describes the dependence of the rate of hydrolytic and synthetic reactions on the composition of the reaction system. The kinetic parameters determined from the progress curves proved very close to those obtained by the initial rate analysis. The kinetic and thermodynamic constants fitted the Haldane equation.
D000581:Amidohydrolases / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008433:Mathematics; D008715:Methionine / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine; D013816:Thermodynamics
D000596:Amino Acids; C006379:N-acetylmethionine; D008715:Methionine; D000581:Amidohydrolases; C019672:aminoacylase I