Substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate.
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.
Nagaki
Masahiko
M
Department of Materials Science and Technology, Faculty of Science and Technology, Hirosaki University, Aomori 036-8561, Japan. nagaki@cc.hirosaki-u.ac.jp
Miki
Yohei
Y
Nakada
Minori
M
Kawakami
Jun
J
Kitahara
Haruo
H
Maki
Yuji
Y
Gotoh
Yoshinori
Y
Nishino
Tokuzo
T
Koyama
Tanetoshi
T
D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D006094:Gram-Positive Bacteria / Q000201:enzymology*; D045782:Hemiterpenes / Q000737:chemistry*; D010755:Organophosphates / Q000737:chemistry*; D013379:Substrate Specificity; D016945:Sulfolobus acidocaldarius / Q000201:enzymology*
C499975:4-methyl-4-pentenyl diphosphate; D045782:Hemiterpenes; D010755:Organophosphates; D019883:Alkyl and Aryl Transferases