Evidence for Nonproductive Binding Subsites within the Active Site of Papain

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Abstract
The reactions of several alkylating reagents with the sulfhydryl group in papain have been studied in the presence of varying concentrations of the competitive inhibitor α-N-benzoyl-D-arginine ethyl ester. The ratio of the alkylation rate constant of the papain – α-N-benzoyl-D-arginine ethyl ester complex to the rate constant with free papain is 4.3, 1.2, and 0.0 for the alkylating agents 1-chloro-3-tosylamido-4-phenyl-2-butanone, N-ethylmaleimide, and 1-chloro-3-tosylamido-7-amino-2-heptanone, respectively. These results are rationalized, along with data for the effect of α-N-benzoyl-L-arginine ethyl ester, in terms of nonproductive binding.

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