title: Kinetic studies of the urokinase-catalysed conversion of NH2-terminal glutamic acid plasminogen to plasmin.
abstract: Initial velocities for the urokinase (EC 3.4.99.26)-catalysed conversion of glutamic acid plasminogen to plasmin (EC 3.4.21.7) have been determined at various urokinase and glutamic acid plasminogen concentrations. As has been found for the corresponding reaction with lysine plasminogen this conversion obeys the Michaelis rate equation. The apparent Michaelis constants are of the same order of magnitude for lysine and glutamic acid plasminogens. The difference in conversion rates for the reactions has been shown to be connected with their having different catalytic constants. The data were analysed according to two reaction schemes, in one of which only one peptide bond is split during the glutamic acid plasminogen-plasmin conversion and in the other of which the cleavage of two peptide bonds with the obligatory formation of an intermediate plasminogen is assumed. The results favour the former.
mesh_terms: D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism*; D005341:Fibrinolysin; D005971:Glutamates; D006801:Humans; D007700:Kinetics; D008433:Mathematics; D010958:Plasminogen; D011485:Protein Binding; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
chemical_list: D005971:Glutamates; D010958:Plasminogen; D010450:Endopeptidases; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator