Alkylphenol biotransformations catalyzed by 4-ethylphenol methylenehydroxylase.
4-ethylphenol methylenehydroxylase from Pseudomonas putida JD1 acts by dehydrogenation of its substrate to give a quinone methide, which is then hydrated to an alcohol. It was shown to be active with a range of 4-alkylphenols as substrates. 4-n-propylphenol, 4-n-butylphenol, chavicol, and 4-hydroxydiphenylmethane were hydroxylated on the methylene group next to the benzene ring and produced the corresponding chiral alcohol as the major product. The alcohols 1-(4'-hydroxyphenyl)propanol and 1-(4'-hydroxyphenyl)-2-propen-1-ol, produced by the biotransformation of 4-n-propylphenol and chavicol, respectively, were shown to be R(+) enantiomers. 5-Indanol, 6-hydroxytetralin, 4-isopropylphenol, and cyclohexylphenol, with cyclic or branched alkyl groups, gave the corresponding vinyl compounds as their major products.
Hopper
David J
DJ
Institute of Biological Sciences, University of Wales, Aberystwyth, Ceredigion SY23 3DD, United Kingdom. dvh@aber.ac.uk
Cottrell
Lisa
L
D008401:Gas Chromatography-Mass Spectrometry; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D016958:Pseudomonas putida / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity
D010636:Phenols; C042291:4-ethylphenol; D006899:Mixed Function Oxygenases; C062024:4-ethylphenol methylenehydroxylase