Initial studies of an esterase using a racemic mixture as substrate revealed that the L enantiomer was the true substrate, as it was completely converted into product, whereas the D enantiomer could be recovered unchanged at the end of the reaction. On the basis of this result the kinetics of the reaction were analyzed assuming that the D enantiomer had no effect on the enzyme, and a Michaelis constant for the L enantiomer was estimated to be 2 mM. Subsequent work made it clear that it would have been more reasonable to assume that the D enantiomer was a competitive inhibitor with KI equal to the Km value of the L enantiomer. How should the original Km estimate be revised to take account of this information?
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