A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates.
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.
Haagen
Yvonne
Y
Pharmazeutisches Institut, Eberhard-Karls-Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen, Germany.
Unsöld
Inge
I
Westrich
Lucia
L
Gust
Bertolt
B
Richard
Stéphane B
SB
Noel
Joseph P
JP
Heide
Lutz
L
D024322:Amino Acids, Aromatic / Q000378:metabolism*; D002384:Catalysis; D004122:Dimethylallyltranstransferase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D008274:Magnesium / Q000494:pharmacology*; D008954:Models, Biological; D017368:Protein Prenylation / Q000187:drug effects; D020539:Sequence Analysis, Protein; D012995:Solubility; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D014169:Transformation, Bacterial
D024322:Amino Acids, Aromatic; D004122:Dimethylallyltranstransferase; D008274:Magnesium