Patulin Biosynthesis: The Role of Mixed-Function Oxidases in the Hydroxylation of m-Cresol
作者： Gillian MURPHY , Gunter VOGEL , Gunther KRIPPAHL , Feodor LYNEN
DOI: 10.1111/J.1432-1033.1974.TB03849.X
关键词: Side reaction 、 Cyanide 、 Cytochrome 、 Enzyme 、 Stereochemistry 、 Biosynthesis 、 Chemistry 、 Reductase 、 Hydroxylation 、 Organic chemistry 、 Patulin
摘要: Two hydroxylation reactions of m-cresol, an intermediate in the secondary biosynthesis antibiotic patulin, have been characterised cell-free preparations Penicillium patulum. The ability to convert m-cresol 2,5-dihydroxytoluene and m-hydroxybenzyl alcohol is located separable fractions 105000 × g microsomal pellet. activities had Km values for 80 μM 5 μM, respectively. Both require molecular oxygen NADPH activity. Inhibition hydroxylases by carbon monoxide reversible light with a photochemical action spectrum maximal at 450 nm. Carbon difference spectra mycel extracts show presence absorbing pigments 422 450–455 nm. The enzymes are not appreciably inhibited cyanide but cytochrome c. m-Cresol therefore appears be catalysed typical mixed-function oxidases involving NADPH-dependent reductase pigment like P-450. In studies on utilisation radioactively labelled intermediates, methyl probably represents important reaction sequence leading patulin formation. Ring side functional higher concentrations m-cresol.
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