Styrene metabolism in Exophiala jeanselmei and involvement of a cytochrome P-450-dependent styrene monooxygenase
Autor: | W. Harder, H. J. Doddema, W. N. M. van Heiningen, Huub H. J. Cox, H. Radhoe, B. W. Faber |
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Rok vydání: | 1996 |
Předmět: |
Cytochrome
Stereochemistry Flavin group Phenylacetic acid Applied Microbiology and Biotechnology Styrenes Styrene chemistry.chemical_compound Cytochrome P-450 Enzyme System Exophiala Cytochrome P-450 Enzyme Inhibitors Homogentisic acid Enzyme Inhibitors Air Pollutants Carbon Monoxide Ecology biology Proadifen Exophiala jeanselmei Phenylacetaldehyde dehydrogenase Metyrapone biology.organism_classification Biodegradation Environmental chemistry Biochemistry Spectrophotometry Oxygenases biology.protein NAD+ kinase Research Article Food Science Biotechnology |
Zdroj: | Applied and Environmental Microbiology. 62:1471-1474 |
ISSN: | 1098-5336 0099-2240 |
DOI: | 10.1128/aem.62.4.1471-1474.1996 |
Popis: | The yeast-like fungus Exophiala jeanselmei degrades styrene via initial oxidation of the vinyl side chain to phenylacetic acid, which is subsequently hydroxylated to homogentisic acid. The initial reactions are catalyzed by a NADPH- and flavin adenine dinucleotide-dependent styrene monooxygenase, a styrene oxide isomerase, and a NAD(+)-dependent phenylacetaldehyde dehydrogenase. The reduced CO-difference spectrum of microsomal preparations of styrene-grown cells shows a characteristic absorption maximum at 450 nm, which strongly suggests the involvement of a cytochrome P-450-dependent styrene monooxygenase. Inhibition of styrene monooxygenase activity in cell extracts by cytochrome P-450 inhibitors SKF-525-A, metyrapone, and CO confirms this assumption. |
Databáze: | OpenAIRE |
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