Abstract
Proton inventories (solvent isotope effects in H2O–D2O mixtures) are not detectably different for the hydrolysis of an anilide substrate catalysed by subtilisin and its N155G mutant, despite the fact that this mutation removes a critical hydrogen-bonding interaction supplied by Asn-155 in the oxyanion hole of the enzyme, which stabilizes the transition state of this reaction by an amount equivalent to two orders of magnitude in reaction rate.
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