Structure and Biocatalytic Scope of Coclaurine N ‐Methyltransferase
Abstract: Benzylisoquinoline alkaloids (BIAs) are a structurally diverse family of plant secondary metabolites, which have been exploited to develop analgesics, antibiotics, antitumor agents, and other therapeutic agents. Biosynthesis of BIAs proceeds via a common pathway from tyrosine to (S)‐reticulene at which point the pathway diverges. Coclaurine N‐methyltransferase (CNMT) is a key enzyme in the pathway to (S)‐reticulene, installing the N‐methyl substituent that is essential for the bioactivity of many BIAs. In this paper, we describe the first crystal structure of CNMT which, along with mutagenesis studies, defines the enzymes active site architecture. The specificity of CNMT was also explored with a range of natural and synthetic substrates as well as co‐factor analogues. Knowledge from this study could be used to generate improved CNMT variants required to produce BIAs or synthetic derivatives.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Structure and Biocatalytic Scope of Coclaurine N ‐Methyltransferase ; volume:130 ; number:33 ; year:2018 ; pages:10760-10764 ; extent:5
Angewandte Chemie ; 130, Heft 33 (2018), 10760-10764 (gesamt 5)
- Creator
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Bennett, Matthew R.
Thompson, Mark L.
Shepherd, Sarah A.
Dunstan, Mark S.
Herbert, Abigail J.
Smith, Duncan R. M.
Cronin, Victoria A.
Menon, Binuraj R. K.
Levy, Colin
Micklefield, Jason
- DOI
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10.1002/ange.201805060
- URN
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urn:nbn:de:101:1-2022081806011415320818
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:34 AM CEST
Data provider
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Associated
- Bennett, Matthew R.
- Thompson, Mark L.
- Shepherd, Sarah A.
- Dunstan, Mark S.
- Herbert, Abigail J.
- Smith, Duncan R. M.
- Cronin, Victoria A.
- Menon, Binuraj R. K.
- Levy, Colin
- Micklefield, Jason
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Author Correction: Structure and mechanism of a methyltransferase ribozyme
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