J Agric Food Chem. 2026 May 5. doi: 10.1021/acs.jafc.6c03303. Online ahead of print.

ABSTRACT

Fungal DMATS-type prenyltransferases catalyze the prenylation of diverse natural products, particularly indole derivatives, but also plant metabolites such as flavonoids. The prenyltransferase UcdE from Aspergillus ustus was previously suggested to catalyze ortho-prenylation of the p-terphenyl derivative dihydroxyterphenyllin. Biochemical investigations with recombinant UcdE substantiated this function and proved the importance of the phenyl ortho-dihydroxylation in p-terphenyls. Testing of various flavonoids, hydroxynaphthalenes, and other polyphenols provided further evidence for the prerequisite of an ortho-dihydroxyphenyl moiety for their acceptance by UcdE. Structural analysis revealed exclusive C2′-prenylation of flavonoids, differing clearly from the prenylation positions of most known prenyltransferases at C-6, C-8 or C-3′. The distinguishing properties of UcdE highlight its unprecedented specificity among prenyltransferases as a promising tool for selective biocatalysis, expanding the range of bioactive compounds for pharmaceutical and nutritional applications.

PMID:42083790 | DOI:10.1021/acs.jafc.6c03303