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

Haagen Yvonne | Zendy; Unsöld Inge | Zendy; Westrich Lucia | Zendy; Gust Bertolt | Zendy; Richard Stéphane B. | Zendy; Noel Joseph P. | Zendy; Heide Lutz | Zendy

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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.

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