Versicolorin A hemiacetal, hydroxydihydrosterigmatocystin, and aflatoxin G2 alpha reductase activity in extracts from Aspergillus parasiticus.

Versicolorin A hemiacetal was converted to versicolorin C in cell-free systems from Aspergillus parasiticus. The rate of reaction catalyzed by the 35-70% ammonium sulfate fraction was 0.43 nmol min-1 mg-1 with NADPH as cosubstrate and 0.17 nmol min-1 mg-1 with NADH at 25 degrees C at pH 7.4. The product from incubation of 17-hydroxy-16,17-dihydrosterigmatocystin with the 35-70% ammonium sulfate fraction and NADPH was a polar compound which was converted to dihydrosterigmatocystin by 0.4 M HCl. The polar compound is proposed to be the 14,17-hydrated open-chain derivative of dihydrosterigmatocystin. Aflatoxin G2 alpha was also reduced in this system to a polar product tentatively identified as the 13,16-hydrated open-chain derivative of AFG2. The reductase activity may be involved in the formation of reduced intermediates and aflatoxins in cultures of A. parasiticus.