Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis
Article first published online: 25 APR 2007
The Plant Journal
Volume 50, Issue 5, pages 902–910, June 2007
How to Cite
Hansen, B. G., Kliebenstein, D. J. and Halkier, B. A. (2007), Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis. The Plant Journal, 50: 902–910. doi: 10.1111/j.1365-313X.2007.03101.x
- Issue published online: 25 APR 2007
- Article first published online: 25 APR 2007
- Received 22 December 2006; revised 12 February 2007; accepted 16 February 2007.
- flavin monooxygenase
The cancer-preventive activity of cruciferous vegetables is commonly attributed to isothiocyanates resulting from the breakdown of the natural products glucosinolates (GSLs). Sulforaphane, the isothiocyanate derived from 4-methylsulfinylbutyl GSL, is thought to be the major agent conferring cancer-preventive properties, whereas the isothiocyanate of 4-methylthiobutyl GSL does not have the same activity. We report the identification of an Arabidopsis flavin-monooxygenase (FMO) enzyme, FMOGS-OX1, which catalyzes the conversion of methylthioalkyl GSLs into methylsulfinylalkyl GSLs. This is evidenced by biochemical characterization of the recombinant protein, and analyses of the GSL content in FMOGS-OX1 overexpression lines and an FMOGS-OX1 knock-out mutant of Arabidopsis. The FMOGS-OX1 overexpression lines show almost complete conversion of methylthioalkyl into methylsulfinylalkyl GSLs, with an approximately fivefold increase in 4-methylsulfinylbutyl GSL in seeds. Identification of FMOGS-OX1 provides a molecular tool for breeding of Brassica vegetable crops with increased levels of this important GSL, which has implications for production of functional foods enriched with the cancer-preventive sulforaphane.