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Entry URI http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u16024588i
Entry name Kim Tae-Wuk et al. 2005 Aug. Plant Cell 17(8):2397-412.
Title Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer-Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis.
Authors Chang Soo Chul|Hwang Jung-Yun|Joo Se-Hwan|Kim Seong-Ki|Kim Tae-Wuk|Kim Young-Soo|Lee June Seung|Takatsuto Suguru
Abstract The conversion of castasterone (CS) to brassinolide (BL), a Baeyer-Villiger oxidation, represents the final and rate-limiting step in the biosynthesis of BL in plants. Heterologously expressed Arabidopsis thaliana CYP85A2 in yeast mediated the conversion of CS to BL as well as the C-6 oxidation of brassinosteroids (BRs). This indicated that CYP85A2 is a bifunctional enzyme that possesses BR C-6 oxidase and BL synthase activity. CYP85A2 is thus a cytochrome P450 that mediates Baeyer-Villiger oxidation in plants. Biochemical, physiological, and molecular genetic analyses of Arabidopsis CYP85A2 loss-of-function and overexpression lines demonstrated that CS has to be a bioactive BR that controls the overall growth and development of Arabidopsis plants. Mutant studies also revealed that BL may not always be necessary for normal growth and development but that Arabidopsis plants acquire great benefit in terms of growth and development in the presence of BL.
Pubmed ID 16024588
Journal The Plant cell
Volume 17
Issue 8
Pages 2397-412
Publication date 2005 Aug
Num of phenotype gene 0