Allosteric effects of some antifibrinolytic amino acids on the catalytic activity of human plasmin.
The effects of L-lysine, 6-aminohexanoic acid, and trans-4-aminomethylcy-clohexane-1-carboxylic acid on the catalytic activity of plasmin (EC 3.4.21.7) have been investigated. The kinetics of the plasmin-catlysed hydrolysis of alpha-N-benzoyl-L-arginine ethyl ester in the presence of these compounds have been studied at a number of different concentrations of the three modifiers. They each exert two effects on the reaction, an activation and an inhibition, the concentration dependencies of which are markedly different. They must therefore arise from two different interactions between plasmin and the modifier. The inhibition is competitive, so that it most probably results from direct interaction at the catalytic site. The activation is kinetically non-competitive. The experimental observations seem to be explained best by assuming that L-lysine and certain analogous compounds function as both allosteric modifiers and competitive inhibitors of plasmin.
D000494:Allosteric Regulation; D000495:Allosteric Site; D015119:Aminocaproic Acid / Q000494:pharmacology; D000933:Antifibrinolytic Agents / Q000494:pharmacology*; D001665:Binding Sites; D002384:Catalysis; D004789:Enzyme Activation; D005341:Fibrinolysin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008239:Lysine / Q000494:pharmacology*; D008433:Mathematics; D014148:Tranexamic Acid / Q000494:pharmacology
D000933:Antifibrinolytic Agents; D014148:Tranexamic Acid; D005341:Fibrinolysin; D008239:Lysine; D015119:Aminocaproic Acid