In order to develop synthetic methods for biologically active homoallylic terpene sulfates, we examined the applicability and substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate (homoIPP).
The reaction of dimethylallyl diphosphate with homoIPP by use of
Bacillus stearothermophilus (all-
trans)-farnesyl diphosphate synthase resulted in efficient yields of
cis-(yield: 45.9%) and
trans-4,8-dimethylnona-3,7-dien-1-ol (homoGOH, 25.5%), which has a carbon skeleton of 4,8-dimethylnona-3-en-1-sulfate, an antiproliferative compound from a marine organism (Aiello, A.
et al.,
Tetrahedron,
53, 11489–11492 (1997)). The homoIPP was found to be also active as a homoallylic substrate in place of isopentenyl diphosphate for
Sulfolobus acidocaldarius geranylgeranyl diphosphate synthase to give diphosphate of
cis- and
trans-4,8,12-trimethyltrideca-3,7,11-trien-1-ol, for
Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase to give
cis- and
trans-4,8,12,16-tetramethylheptadeca-3,7,11,15-tetraen-1-ol (homoGGOH), and for
Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase to give
cis-homoGGOH exclusively.
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