Recombinant glycerol dehydratase ofKlebsiella pneumoniae was purified to homogeneity. The subunit composition of the enzyme was most probablya2b2c2 .When(R)- and (S)-propane-1,2-diolswere used independently as substrates, the rate with the (R)-enantiomer was times faster than that with the (S)-isomer. In contrast to diol dehydratase,an iso-functional enzyme,the affinity of the enzyme for the (S)-isomer was essentially the same or only slightly higher than that for the (R)-isomer (Km(R) /Km(S) ¼). .
