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http://purl.uniprot.org/cit... | rdfs:comment | 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, FMO(GS-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 FMO(GS-OX1) overexpression lines and an FMO(GS-OX1) knock-out mutant of Arabidopsis. The FMO(GS-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 FMO(GS-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. | lld:uniprot |
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http://purl.uniprot.org/cit... | uniprot:name | Plant J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Halkier B.A. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Kliebenstein D.J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Hansen B.G. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:date | 2007 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:pages | 902-910 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:title | Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:volume | 50 | lld:uniprot |
http://purl.uniprot.org/cit... | dc-term:identifier | doi:10.1111/j.1365-313X.2007.03101.x | lld:uniprot |
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