Thermodynamic parameters of the formation of the enzyme [C3 convertase] substrate complex

Range Table - link
Organism Human Homo sapiens
Reference Vogel CW, Müller-Eberhard HJ. The cobra venom factor-dependent C3 convertase of human complement. A kinetic and thermodynamic analysis of a protease acting on its natural high molecular weight substrate. J Biol Chem. 1982 Jul 25 257(14):8292-9 p.8296 table IVPubMed ID6919543
Method Abstract: "Enzymes of the complement system exhibit, unlike most other proteases, a high substrate specificity, hydrolyzing only a single peptide bond in their protein substrates. This property allowed the performance of a detailed analysis of the enzymatic activity of a protease acting on its natural high molecular weight substrate."
Comments P.8296 left column 3rd paragraph: "The standard enthalpy, ΔH˚, of the formation of the enzyme-substrate complex was calculated from the slope of the linear van't Hoff plot and a value of 5300 cal/mol was obtained. The standard Gibbs energies, ΔG˚, for formation of the complex are listed in Table IV, and the standard entropy, ΔS˚, was found to be 39.71 cal/mol/K."
Entered by Uri M
ID 114398