Kinetic parameters of C3 hydrolysis by the CVF [cobra venom factor]-dependent C3 convertase

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.8295 table IPubMed 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.8295 left column 3rd paragraph: "Table I lists the kinetic parameters determined for each of the four temperatures. Mean values and standard deviations have been calculated for the parameters Km, turnover number, and ko =v/[S] which were determined by several individual experiments. The other parameters were derived from these mean values. Since the CVF-dependent C3 convertase has only one catalytic subunit/molecule, the turnover number is identical with the catalytic center activity. Up to a C3 concentration of about 3×10^-6M, the substrate turnover can be described as a first order reaction. The apparent first order rate constants, ko, were determined by two methods as described under “Experimental Procedures” and are also listed in Table I."
Entered by Uri M
ID 114395