ArticleAngewandte Chemie (International ed. in English)2018
Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- A Golgi-localized N-methyltransferase and reversible aldo-keto reductases coordinate dual terminal routes in galanthamine biosynthesis.The Plant journal : for cell and molecular biology · 2026Article
- Biosynthesis of benzylisoquinoline alkaloids and its evolution in plants.Plant communications · 2026Review
- Neuroprotective Potential of Major Alkaloids fromInternational journal of molecular sciences · 2025Review
- Metabolomic Insights into Sexual Multi-Morphism of Sinomenine Accumulation inPlants (Basel, Switzerland) · 2025Article
- Convergent evolution of berberine biosynthesis.Science advances · 2024Article
- Modular assembly of an artificially concise biocatalytic cascade for the manufacture of phenethylisoquinoline alkaloids.Nature communications · 2024Article
- Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Elucidation of the (R)-enantiospecific benzylisoquinoline alkaloid biosynthetic pathways in sacred lotus (Nelumbo nucifera).Scientific reports · 2023Article
- Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.Molecules (Basel, Switzerland) · 2022Review
- Review
- Multienzyme One-Pot Cascades Incorporating Methyltransferases for the Strategic Diversification of Tetrahydroisoquinoline Alkaloids.Angewandte Chemie (International ed. in English) · 2021Article
- Multienzyme One-Pot Cascades Incorporating Methyltransferases for the Strategic Diversification of Tetrahydroisoquinoline Alkaloids.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Biosynthesis and synthetic biology of psychoactive natural products.Chemical Society reviews · 2021Review
- Cross-linking of a polyketide synthase domain leads to a recyclable biocatalyst for chiral oxygen heterocycle synthesis.RSC advances · 2021Article
- Enzyme-mediated bioorthogonal technologies: catalysts, chemoselective reactions and recent methyltransferase applications.Current opinion in biotechnology · 2021Review
- Back to the plant: overcoming roadblocks to the microbial production of pharmaceutically important plant natural products.Journal of industrial microbiology & biotechnology · 2020Review
- Engineering Orthogonal Methyltransferases to Create Alternative Bioalkylation Pathways.Angewandte Chemie (International ed. in English) · 2020Article
- Biosynthesis of plant tetrahydroisoquinoline alkaloids through an imine reductase route.Chemical science · 2020Article
- Structure-function studies of tetrahydroprotoberberineThe Journal of biological chemistry · 2019Article
- Molecular Origins of Functional Diversity in Benzylisoquinoline Alkaloid Methyltransferases.Frontiers in plant science · 2019Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.