| Abstract: | A cell-free enzyme system from cultures of Fusarium culmorum catalyses the 12,13-epoxidation of semi-synthetic 9 beta,10 beta-epoxytrichodiene to 9 beta,10 beta;12,13-diepoxytrichodiene. This enzyme activity may be involved in the biosynthesis of trichothecene mycotoxins and since the 12,13-epoxide is known to be essential for toxicity, the enzyme activity probably confers the toxic properties associated with this group of mycotoxins. The epoxidase requires NADPH and molecular oxygen, is inhibited by carbon monoxide, and thus appears to be a cytochrome P-450-dependent mono-oxygenase. Whole cell cultures of the fungus carry out the same biotransformation, and in addition hydroxylate the diepoxide product at position 3, yielding 3 alpha-hydroxy-9 beta,10 beta;12,13-diepoxytrichodiene. |
