The substrate specificity of acetimidylated (A-HLADH) and hydroxybutyrimidylated horse liver alcohol dehydrogenase (HB-HLADH) has been evaluated for the ethanol–acetaldehyde, trans-2-hexenol–trans-2-hexenal, furfural–furfuryl alcohol, benzaldehyde–benzyl alcohol, cyclobutanol–cyclobutanone, cyclopentanol–cyclopentanone, cyclohexanol–cyclohexanone, and cycloheptanol–cycloheptanone substrate couples. The pH-optima of A- and HB-HLADH are similar to that of native enzyme (∼pH 7) for the reduction mode, but are displaced from the broad ∼8–10.5 range for the native enzyme to ∼11.8 for the modified enzymes in the oxidative mode. However, because of coenzyme instability, the practical pH optimum for oxidations remains 9 for both native and modified HLADH's. The modified enzymes provide limited synthetic advantages for the substrates evaluated.
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Jones et al. (1979) studied this question.