Cholinesterase: substrate inhibition and substrate activation
Copyright policy )Cholinesterase: substrate inhibition and substrate activation
The relationship between activities and substrate concentrations (pS-curves) was analysed for reactions of acetylcholinesterase (EC 3.1.1.7) and butyrylcholinesterase (EC 3.1.1.8). Catalytic constants Km, Kss, Vm, n and b were calculated from the Michaelis, Haldane, Hill and Webb equations in order to assess whether a given substrate also acts as an inhibitor or activator. It is suggested that the term substrate inhibition should only be attributed to substrates revealing bell-shaped pS-curves, while the terms apparent substrate inhibition or apparent substrate activation should relate to calculated values of the catalytic constants.
Kinetics, Butyrylcholinesterase, Hydrolysis, Acetylcholinesterase, acetylcholinesterase; butyrylcholinesterase; catalytic constants, Animals, Humans, Models, Biological, Catalysis, Substrate Specificity
Kinetics, Butyrylcholinesterase, Hydrolysis, Acetylcholinesterase, acetylcholinesterase; butyrylcholinesterase; catalytic constants, Animals, Humans, Models, Biological, Catalysis, Substrate Specificity
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