Substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate.

Masahiko Nagaki, Yohei Miki, Minori Nakada, Jun Kawakami, Haruo Kitahara, Yuji Maki, Yoshinori Gotoh, Tokuzo Nishino, Tanetoshi Koyama

Department of Materials Science and Technology, Faculty of Science and Technology, Hirosaki University, Aomori 036-8561, Japan. nagaki@cc.hirosaki-u.ac.jp

Bioscience, biotechnology, and biochemistry 2004 Oct

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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.

Citation

Masahiko Nagaki, Yohei Miki, Minori Nakada, Jun Kawakami, Haruo Kitahara, Yuji Maki, Yoshinori Gotoh, Tokuzo Nishino, Tanetoshi Koyama. Substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate. Bioscience, biotechnology, and biochemistry. 2004 Oct;68(10):2070-5