Abstract
1. 1. Using synthetic arginines as substrates, steady-state kinetic studies showed a deviation from Michaelis-Menten kinetics for esterase E-I purified from the venom of Bitis gabonica. Graphical analysis indicated a rate equation of at least a degree of 3:3. 2. 2. pH variation of the kinetic parameters indicated the involvement of groups with pK values of ~7 and ~9 which had to be in the ionic form for activity. 3. 3. Solvent isotope studies suggested transition states where proton transfer or reorganization was the rate-limiting step of proteolytic catalysis. A single protogenic site was postulated. 4. 4. Temperature effects on the enzymic reaction showed a significant reduction in entropy loss upon formation of the transition state with both esters and extended tail polypeptide-analides in comparison with the activation entropy for benzoyl- l-arginine p-nitroanalide.
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