Biochemical and Structural Insights of the <i>N</i>-Methyltransferase CyaF in Cyanogramide Biosynthesis

<i>N</i>-Methyltransferases involved in indole methylation have seldom been discovered in natural product biosynthesis. This study focuses on the enzyme CyaF, which catalyzes a critical <i>N</i>-methylation step of indole in the β-carboline skeleton during cyanogramide biosynthesis. Seven β-carboline analogues (<b>3</b>-<b>9</b>) were isolated from the recombinant strain <i>Streptomyces coelicolor</i> YF11/<i>cyaABC</i>, including three new compounds (<b>5</b>-<b>7</b>). <i>In vitro</i> assays revealed CyaF's substrate flexibility. The crystal structure of the CyaF/<i>S</i>-adenosyl-L-homocysteine (SAH) complex, combined with the AlphaFold-predicted model and site-directed mutagenesis, elucidated the catalytic mechanism and structural features that enable CyaF to accommodate diverse substrates, highlighting its potential for biocatalytic applications.

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Publication Details

Journal
Journal of Natural Products
Published
2025-03-07
DOI
https://doi.org/10.1021/acs.jnatprod.4c01391
Citations
1
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
1.23

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article

Biochemical and Structural Insights of the N-Methyltransferase CyaF in Cyanogramide Biosynthesis

Weiming Zhu, Hanning Zhu, Yiguang Zhu, Liping Zhang et al.
1 citations
Journal of Natural Products
Enzyme Production and Characterization
1.23
article

Biochemical and Structural Insights of the N-Methyltransferase CyaF in Cyanogramide Biosynthesis

Weiming Zhu, Hanning Zhu, Yiguang Zhu, Liping Zhang, Changsheng Zhang, Ruijie Chen, Qingbo Zhang, Chunyan Fang
article en
1 citations

Abstract

<i>N</i>-Methyltransferases involved in indole methylation have seldom been discovered in natural product biosynthesis. This study focuses on the enzyme CyaF, which catalyzes a critical <i>N</i>-methylation step of indole in the β-carboline skeleton during cyanogramide biosynthesis. Seven β-carboline analogues (<b>3</b>-<b>9</b>) were isolated from the recombinant strain <i>Streptomyces coelicolor</i> YF11/<i>cyaABC</i>, including three new compounds (<b>5</b>-<b>7</b>). <i>In vitro</i> assays revealed CyaF's substrate flexibility. The crystal structure of the CyaF/<i>S</i>-adenosyl-L-homocysteine (SAH) complex, combined with the AlphaFold-predicted model and site-directed mutagenesis, elucidated the catalytic mechanism and structural features that enable CyaF to accommodate diverse substrates, highlighting its potential for biocatalytic applications.

Journal of Natural ProductsVol. 88(3)
Ministry of Education of the People's Republic of China (CN), Chinese Academy of Sciences (CN), Institute of Oceanology (CN), South China Sea Institute Of Oceanology (CN), Institute of Deep-Sea Science and Engineering (CN), University of Chinese Academy of Sciences (CN), State Key Laboratory of Tropical Oceanography, Ocean University of China (CN)
National Natural Science Foundation of China, Natural Science Foundation of Hainan Province, National Key Research and Development Program of China, Basic and Applied Basic Research Foundation of Guangdong Province
Openalex Percentile: Top 25%
Enzyme Production and Characterization
1.23
DOISourceOpenAlex
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