| 10334943 |
Curtis AJ, Shirk MC, Fall R: Allylic or benzylic stabilization is essential for catalysis by bacterial benzyl alcohol dehydrogenases. Biochem Biophys Res Commun. 1999 May 27;259(1):220-3.
Benzyl alcohol dehydrogenase from Acinetobacter calcoaceticus (AC-BADH) and TOL plasmid-encoded benzyl alcohol dehydrogenase from Pseudomonas putida (TOL-BADH) have previously been shown to oxidize a variety of aromatic alcohols but not aliphatic substrates. Here, we have expressed the genes for AC-BADH and TOL-BADH in Escherichia coli, purified the resulting over-expressed enzymes, and shown that each is an effective catalyst of both benzylic and allylic alcohol oxidation, but not of oxidation of nonallylic analogs. Enzyme specificity (kcat/Km) for both enzymes was higher with an aliphatic, allylic alcohol (3-methyl-2-buten-1-ol) than with benzyl alcohol. These results suggest that bacterial benzyl alcohol dehydrogenases use the resonance stabilization provided by allylic and benzylic alcohols to promote catalysis. |
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