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A soluble, magnesium‐independent prenyltransferase catalyzes reverse and regular C ‐prenylations and O ‐prenylations of aromatic substrates
Author(s) -
Haagen Yvonne,
Unsöld Inge,
Westrich Lucia,
Gust Bertolt,
Richard Stéphane B.,
Noel Joseph P.,
Heide Lutz
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.031
Subject(s) - prenyltransferase , prenylation , chemistry , divalent , stereochemistry , enzyme , catalysis , monomer , substrate (aquarium) , streptomyces , biosynthesis , metal , biochemistry , organic chemistry , biology , bacteria , ecology , genetics , polymer
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 Mg 2+ 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.