ArticlePlant biotechnology journal2025
Elucidating the enzyme network driving Amaryllidaceae alkaloids biosynthesis in Leucojum aestivum.
Article in Plant biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Amaryllidaceae Alkaloids and Isoquinoline Alkaloids: A Perspective on Historical Approaches to Pathway Elucidation.Plants (Basel, Switzerland) · 2026Review
- Two roads to galanthamine turn out to be one.The Plant journal : for cell and molecular biology · 2026Article
- 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
- Amaryllidaceae Alkaloids and Phenolic Acids Identification inMolecules (Basel, Switzerland) · 2026Article
- Article
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Authors and funding
7 authors.
Funding
Abstract
Amaryllidaceae alkaloids (AAs) are diverse bioactive metabolites with significant pharmaceutical potential, derived from 4'-O-methylnorbelladine (4'OM). The biosynthesis of these compounds involves the condensation of tyramine and 3,4-dihydroxybenzaldehyde by norbelladine synthase (NBS) and/or noroxomaritidine/norcraugsodine reductase (NR), followed by O-methylation. Cytochrome P450 enzymes, particularly the CYP96T family, introduce further structural diversity through C-C couplings, resulting in lycorine, galanthamine and crinine cores. Despite their importance, the exact biosynthetic pathways remain poorly defined. In this study, we describe key enzymes from Leucojum aestivum (La), providing crucial insight into AA biosynthesis. Transient expression in Nicotiana benthamiana demonstrated that LaNBS and LaNRII catalyse the conversion of tyramine and 3,4-dihydroxybenzaldehyde to norbelladine, which is subsequently O-methylated by a norbelladine-4'-O-methyltransferase (LaN4'OMT) in planta. Co-agroinfiltration of LaNBS, LaNRII, LaN4'OMT and LaCYP96T1 resulted in the production of various phenol-coupled products, with lycorine as the predominant compound, alongside haemanthamine, crinine/vittatine and norgalanthamine. This study identifies LaCYP96T1 and LaCYP96T2 as the first monocot enzymes capable of catalysing all three regioselective C-C phenol couplings and also highlights the substrate promiscuity of LaNRII. The findings not only elucidate critical steps in AA biosynthesis but also open new avenues for biotechnological application in producing valuable alkaloids, offering potential for novel drug development.
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