Enzymatic formation of indole-containing unnatural cyclic polyprenoids by bacterial squalene:hopene cyclase.
[reaction: see text] Two indole-containing substrate analogues, in which a C20 isoprene unit is connected to indole (3-(geranylgeranyl)indole and 3-(farnesyldimethylallyl)indole), were synthesized and tested for enzymatic cyclization by squalene:hopene cyclase from Alicyclobacillus acidocaldarius. Interestingly, 3-(geranylgeranyl)indole was not a substrate for the bacterial squalene cyclase, while 3-(farnesyldimethylallyl)indole was efficiently converted to a 2:1 mixture of unnatural novel products.
Tanaka
Hideya
H
School of Pharmaceutical Sciences and the COE 21 Program, University of Shizuoka, Shizuoka 422-8526, Japan.
Noguchi
Hiroshi
H
Abe
Ikuro
I
D001407:Bacillus / Q000201:enzymology*; D003500:Cyclization; D007211:Indoles / Q000737:chemistry / Q000378:metabolism*; D008190:Lyases / Q000378:metabolism*; D015394:Molecular Structure; D011084:Polycyclic Aromatic Hydrocarbons / Q000737:chemistry / Q000378:metabolism*; D013185:Squalene / Q000737:chemistry / Q000378:metabolism
D007211:Indoles; D011084:Polycyclic Aromatic Hydrocarbons; D013185:Squalene; D008190:Lyases; C022651:squalene cyclase