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To study the mechanism of enzyme action, cyclo(His–Glu–Cys-d-Phe–Gly)2 was prepared as an esterase model from the corresponding linear decapeptide by the azide methods. The esterase-like activity of this cyclic decapeptide in reaction to p-nitrophenyl acetate was three times greater than that of the linear decapeptide, the curve of the catalytic coefficient versus the different pH is of a bell type, and the optimum pH was recorded at about 7.6. The kinetics of the hydrolysis obeyed Michaelis-Menten’s typical equation.
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Nakajima et al. (1973) studied this question.
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