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

被引:50
作者
Haagen, Yvonne
Unsoeld, Inge
Westrich, Lucia
Gust, Bertolt
Richard, Stephane B.
Noel, Joseph P.
Heide, Lutz
机构
[1] Univ Tubingen, Inst Pharmazeut, D-72076 Tubingen, Germany
[2] Salk Inst Biol Studies, Jack Skirball Chem Biol & Proteom Lab, La Jolla, CA 92037 USA
关键词
prenyltransferase; reverse prenylation; furanonaphthoquinone; Streptomyces;
D O I
10.1016/j.febslet.2007.05.031
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2889 / 2893
页数:5
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