Abstract
The late stage of patulin biosynthesis was studied using cell-free preparation of Penicillium patulum NRRL 2159A. The substrate for the ring cleavage reaction was established to be gentisyl alcohol, which was converted into patulin by a microsomal enzyme(s). Incubation of [1'-14C, 3H2]-gentisyl alcohol with the microsomal preparation revealed that one of the carbinol protons of this substrate is retained in patulin. This answers the long-standing question why the side chain protons of aromatic intermediates are not incorporated into patulin in feeding experiments.
