A soluble, magnesium‐independent prenyltransferase catalyzes reverse and regular C‐prenylations and O‐prenylations of aromatic substrates

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Abstract
Fnq26 from Streptomyces cinnamonensis DSM 1042 is a new member of the recently identified CloQ/Orf2 class of prenyltransferases. The enzyme was overexpressed in E. coli and purified to apparent homogeneity, resulting in a soluble, monomeric protein of 33.2 kDa. The catalytic activity of Fnq26 is independent of the presence of Mg2+ or other divalent metal ions. With flaviolin (2,5,7‐trihydroxy‐1,4‐naphthoquinone) as substrate, Fnq26 catalyzes the formation of a carbon–carbon‐bond between C‐3 (rather than C‐1) of geranyl diphosphate and C‐3 of flaviolin, i.e. an unusual “reverse” prenylation. With 1,3‐dihydroxynaphthalene and 4‐hydroxybenzoate as substrates Fnq26 catalyzes O‐prenylations.