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The interaction of α-chymotrypsin with isosteric substrates of different charge type

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PMC
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Abstract

1. The synthesis of three substrates of α-chymotrypsin of closely similar steric requirements but different charge type is reported. 2. The interaction of these compounds [SS-dimethyl-(l-3-carboxymethyl-3-acetamido)propyl sulphonium iodide, l-2-acetamido-5-methylhexanoic acid methyl ester and N-acetyl-l-glutamic acid α-methyl ester] with α-chymotrypsin has been studied. 3. For the charged substrates, values of k0 are two orders of magnitude smaller than, and values of Km two orders of magnitude larger than, the corresponding values for the uncharged isostere. 4. The results are interpreted in terms of the known specificity of the enzyme, and the relationship between binding and kinetic specificities is discussed.

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