CYP71B15 (PAD3) catalyzes the final step in camalexin biosynthesis

Regina Schuhegger, Majse Nafisi, Madina Mansourova, Bent Larsen Petersen, Carl Erik Olsen, Aleš Svatoš, Barbara Ann Halkier, Erich Glawischnig

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

195 Citas (Scopus)

Resumen

Camalexin represents the main phytoalexin in Arabidopsis (Arabidopsis thaliana). The camalexin-deficient phytoalexin deficient 3 (pad3) mutant has been widely used to assess the biological role of camalexin, although the exact substrate of the cytochrome P450 enzyme 71B15 encoded by PAD3 remained elusive. 2-(Indol-3-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid (dihydrocamalexic acid) was identified as likely intermediate in camalexin biosynthesis downstream of indole-3-acetaldoxime, as it accumulated in leaves of silver nitrate-induced pad3 mutant plants and it complemented the camalexin-deficient phenotype of a cyp79b2/cyp79b3 double-knockout mutant. Recombinant CYP71B15 heterologously expressed in yeast catalyzed the conversion of dihydrocamalexic acid to camalexin with preference of the (S)-enantiomer. Arabidopsis microsomes isolated from leaves of CYP71B15-overexpressing and induced wild-type plants were capable of the same reaction but not microsomes from induced leaves of pad3 mutants. In conclusion, CYP71B15 catalyzes the final step in camalexin biosynthesis.

Idioma originalInglés
Páginas (desde-hasta)1248-1254
Número de páginas7
PublicaciónPlant Physiology
Volumen141
N.º4
DOI
EstadoPublicada - ago. 2006
Publicado de forma externa

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