Abstract
Reversible inhibition phenomena are analyzed for enzymatic systems involving covalent intermediates, where the inhibitor can bind to the pure enzyme, the Henri-Michaelis complex or the covalent intermediate, or to two or three of these enzyme forms. Classical competitive, non-competitive or un-competitive phenomena can be observed in some cases but unexpected features are also observed. Complex phenomena sometimes prevail where increased kcat/Km values can be accompanied by decreased or increased kcat values.
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