A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis

The biosynthesis of the antitumour antibiotic CC-1065 includes formation of a cyclopropane. Here, the authors identify the two enzymes that work together to catalyze this reaction, a radical S-adenosyl-l-methionine enzyme and a methyltransferase, and propose a mechanism for the cyclopropanation.

Bibliographic Details
Main Authors: Wen-Bing Jin, Sheng Wu, Xiao-Hong Jian, Hua Yuan, Gong-Li Tang
Format: Article
Language:English
Published: Nature Portfolio 2018-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-05217-1
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author Wen-Bing Jin
Sheng Wu
Xiao-Hong Jian
Hua Yuan
Gong-Li Tang
author_facet Wen-Bing Jin
Sheng Wu
Xiao-Hong Jian
Hua Yuan
Gong-Li Tang
author_sort Wen-Bing Jin
collection DOAJ
description The biosynthesis of the antitumour antibiotic CC-1065 includes formation of a cyclopropane. Here, the authors identify the two enzymes that work together to catalyze this reaction, a radical S-adenosyl-l-methionine enzyme and a methyltransferase, and propose a mechanism for the cyclopropanation.
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spelling doaj.art-edcd713c52a44ba79dc899e965e8716e2022-12-21T21:35:24ZengNature PortfolioNature Communications2041-17232018-07-019111010.1038/s41467-018-05217-1A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesisWen-Bing Jin0Sheng Wu1Xiao-Hong Jian2Hua Yuan3Gong-Li Tang4State Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of SciencesThe biosynthesis of the antitumour antibiotic CC-1065 includes formation of a cyclopropane. Here, the authors identify the two enzymes that work together to catalyze this reaction, a radical S-adenosyl-l-methionine enzyme and a methyltransferase, and propose a mechanism for the cyclopropanation.https://doi.org/10.1038/s41467-018-05217-1
spellingShingle Wen-Bing Jin
Sheng Wu
Xiao-Hong Jian
Hua Yuan
Gong-Li Tang
A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
Nature Communications
title A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
title_full A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
title_fullStr A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
title_full_unstemmed A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
title_short A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
title_sort radical s adenosyl l methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis
url https://doi.org/10.1038/s41467-018-05217-1
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