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Reeve CD, Carver MA, Hopper DJ: Stereochemical aspects of the oxidation of 4-ethylphenol by the bacterial enzyme 4-ethylphenol methylenehydroxylase. Biochem J. 1990 Aug 1;269(3):815-9.
The O2-independent hydroxylase 4-ethylphenol methylenehydroxylase (4EPMH) from Pseudomonas putida JD1 catalysed the complete conversion of 4-ethylphenol into 1-(4-hydroxyphenyl) ethanol together with a small amount of 4-hydroxyacetophenone, but with no formation of the side product 4-vinylphenol reported to be formed when the similar enzyme p-cresol methylhydroxylase (PCMH) catalyses this reaction. The enantiomer of 1-(4-hydroxyphenyl) ethanol produced by 4EPMH was R (+) when horse heart cytochrome c or azurin was used as electron acceptor for the enzyme. PCMHs from various bacterial strains produced the S (-)-alcohol. Both enantiomers of 1-(4-hydroxyphenyl) ethanol were substrates for conversion into 4-hydroxyacetophenone by 4EPMH, but the S (-)-isomer was preferred. The Km and kcat. were 1.2 mM and 41 s-1 respectively for the S (-)-alcohol and 4.7 mM and 22 s-1 for the R (+)-alcohol. In addition to the 1-(4-hydroxyphenyl) ethanol dehydrogenase activity of 4-EPMH, NAD (+)-linked dehydrogenase activity for both enantiomers of the alcohol was found in extracts of Ps. putida JD1. |
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