O. Kniemeyer et J. Heider, (S)-1-Phenylethanol dehydrogenase of Azoarcus sp strain EbN1, an enzyme ofanaerobic ethylbenzene catabolism, ARCH MICROB, 176(1-2), 2001, pp. 129-135
The initial steps in the anaerobic oxidation of the aromatic hydrocarbon et
hylbenzene by denitrifying bacteria are two sequential dehydrogenation reac
tions of ethylbenzene to (S)-1-phenylethanol and further to acetophenone. T
he enzyme catalysing the second oxidation step, (S)-1-phenylethanol dehydro
genase, was analysed in the denitrifying bacterium Azoarcus sp. strain EbN1
. An NAD(+)-dependent 1-phenylethanol dehydrogenase for each of the enantio
mers of 1-phenylethanol was identified in this bacterium; the two enzymes w
ere induced under different growth conditions. (S)-1-phenylethanol dehydrog
enase from ethylbenzene-grown cells was purified and biochemically characte
rised. The enzyme is a typical secondary alcohol dehydrogenase and consists
of two subunits of 25.5 kDa. The enantioselective enzyme catalyses the oxi
dation of (S)-1-phenylethanol or the reduction of acetophenone and is inhib
ited by high concentrations of (R)-1-phenylethanol. The enzyme exhibits low
apparent K-m values for (S)-1-phenylethanol and acetophenone and is rather
substrate-specific, using only a few chemically similar secondary alcohols
, such as 1-phenylpropanol and isopropanol.