Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY
Plant biosynthetic enzymes rapidly evolve to catalyze specialized reactions. Here, the authors present the crystal structure and mechanism of COSY, the enzyme involved in coumarin biosynthesis of the BAHD-acyltransferase family that catalyzes an intramolecular acyl transfer reaction through a proton...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-36299-1 |
| _version_ | 1828041528841338880 |
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| author | Colin Y. Kim Andrew J. Mitchell David W. Kastner Claire E. Albright Michael A. Gutierrez Christopher M. Glinkerman Heather J. Kulik Jing-Ke Weng |
| author_facet | Colin Y. Kim Andrew J. Mitchell David W. Kastner Claire E. Albright Michael A. Gutierrez Christopher M. Glinkerman Heather J. Kulik Jing-Ke Weng |
| author_sort | Colin Y. Kim |
| collection | DOAJ |
| description | Plant biosynthetic enzymes rapidly evolve to catalyze specialized reactions. Here, the authors present the crystal structure and mechanism of COSY, the enzyme involved in coumarin biosynthesis of the BAHD-acyltransferase family that catalyzes an intramolecular acyl transfer reaction through a proton exchange mechanism. |
| first_indexed | 2024-04-10T17:17:35Z |
| format | Article |
| id | doaj.art-ba81046af1a147e19edddaaedab81596 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-10T17:17:35Z |
| publishDate | 2023-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-ba81046af1a147e19edddaaedab815962023-02-05T12:18:09ZengNature PortfolioNature Communications2041-17232023-02-0114111510.1038/s41467-023-36299-1Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSYColin Y. Kim0Andrew J. Mitchell1David W. Kastner2Claire E. Albright3Michael A. Gutierrez4Christopher M. Glinkerman5Heather J. Kulik6Jing-Ke Weng7Whitehead Institute for Biomedical ResearchWhitehead Institute for Biomedical ResearchDepartment of Biological Engineering, Massachusetts Institute of TechnologyWhitehead Institute for Biomedical ResearchWhitehead Institute for Biomedical ResearchWhitehead Institute for Biomedical ResearchDepartment of Chemical Engineering, Massachusetts Institute of TechnologyWhitehead Institute for Biomedical ResearchPlant biosynthetic enzymes rapidly evolve to catalyze specialized reactions. Here, the authors present the crystal structure and mechanism of COSY, the enzyme involved in coumarin biosynthesis of the BAHD-acyltransferase family that catalyzes an intramolecular acyl transfer reaction through a proton exchange mechanism.https://doi.org/10.1038/s41467-023-36299-1 |
| spellingShingle | Colin Y. Kim Andrew J. Mitchell David W. Kastner Claire E. Albright Michael A. Gutierrez Christopher M. Glinkerman Heather J. Kulik Jing-Ke Weng Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY Nature Communications |
| title | Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY |
| title_full | Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY |
| title_fullStr | Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY |
| title_full_unstemmed | Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY |
| title_short | Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY |
| title_sort | emergence of a proton exchange based isomerization and lactonization mechanism in the plant coumarin synthase cosy |
| url | https://doi.org/10.1038/s41467-023-36299-1 |
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