A new paradigm for biohydroxylation by Beauveria bassiana ATCC 7159

Article abstract of DOI:10.1016/S0040-4020(99)00393-2

The biohydroxylation of a series of amides and related amino, keto and hydrocarbon substrates by the fungal biocatalyst Beauveria bassiana ATCC 7159 has been examined. The product distributions, together with data obtained from selective inhibition experiments using the cyt.P-450 inhibitors isosafrole, 1-aminobenzotriazole and phenylacetylene, suggest that B. bassiana contains a range of hydroxylase enzymes with different substrate specificities. A paradigm is presented for the interpretation of the results of microbial hydroxylation and for the application of existing active site models for B. bassiana.