Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis

Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report two new cytochromes P450 from Brassica rapa (Chinese cabbage) that catalyze unprecedented S-heterocyclizations in cyclobrassinin and spirobra...

Descripción completa

Detalles Bibliográficos
Autores principales: Klein, Andrew P, Sattely, Elizabeth S
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4731101/
https://www.ncbi.nlm.nih.gov/pubmed/26389737
http://dx.doi.org/10.1038/nchembio.1914
_version_ 1782412514158444544
author Klein, Andrew P
Sattely, Elizabeth S
author_facet Klein, Andrew P
Sattely, Elizabeth S
author_sort Klein, Andrew P
collection PubMed
description Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report two new cytochromes P450 from Brassica rapa (Chinese cabbage) that catalyze unprecedented S-heterocyclizations in cyclobrassinin and spirobrassinin biosynthesis. Our results reveal the first genetic and biochemical insights into the biosynthesis of a prominent pair of dietary metabolites, and have implications for pathway discovery across >20 recently sequenced crucifers.
format Online
Article
Text
id pubmed-4731101
institution National Center for Biotechnology Information
language English
publishDate 2015
record_format MEDLINE/PubMed
spelling pubmed-47311012016-05-01 Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis Klein, Andrew P Sattely, Elizabeth S Nat Chem Biol Article Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report two new cytochromes P450 from Brassica rapa (Chinese cabbage) that catalyze unprecedented S-heterocyclizations in cyclobrassinin and spirobrassinin biosynthesis. Our results reveal the first genetic and biochemical insights into the biosynthesis of a prominent pair of dietary metabolites, and have implications for pathway discovery across >20 recently sequenced crucifers. 2015-09-21 2015-11 /pmc/articles/PMC4731101/ /pubmed/26389737 http://dx.doi.org/10.1038/nchembio.1914 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Klein, Andrew P
Sattely, Elizabeth S
Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title_full Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title_fullStr Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title_full_unstemmed Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title_short Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis
title_sort two cytochromes p450 catalyze s-heterocyclizations in cabbage phytoalexin biosynthesis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4731101/
https://www.ncbi.nlm.nih.gov/pubmed/26389737
http://dx.doi.org/10.1038/nchembio.1914
work_keys_str_mv AT kleinandrewp twocytochromesp450catalyzesheterocyclizationsincabbagephytoalexinbiosynthesis
AT sattelyelizabeths twocytochromesp450catalyzesheterocyclizationsincabbagephytoalexinbiosynthesis

Ejemplares similares