ArticleAngewandte Chemie (International ed. in English)2022
Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Tuning reductase activity in monoterpene indole alkaloid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Interactomics-driven discovery of alkaloid biosynthetic pathways in kratom.bioRxiv : the preprint server for biology · 2026Article
- Enzymatic epimerization of monoterpene indole alkaloids in kratom.Nature chemical biology · 2026Article
- Protein-Protein Interactions Modulate a Key Branch Point in Monoterpene Indole Alkaloid Biosynthesis.ACS chemical biology · 2026Article
- A Tight-Knit Family: The Medium-Chain Dehydrogenase/Reductases of Monoterpene Indole Alkaloid Biosynthesis.Biochemistry · 2025Review
- Two ubiquitous aldo-keto reductases in the genus Papaver support a patchwork model for morphine pathway evolution.Communications biology · 2024Article
- The Rauvolfia tetraphylla genome suggests multiple distinct biosynthetic routes for yohimbane monoterpene indole alkaloids.Communications biology · 2023Article
- Preparation of Alcohol Dehydrogenase-Zinc Phosphate Hybrid Nanoflowers through Biomimetic Mineralization and Its Application in the Inhibitor Screening.Molecules (Basel, Switzerland) · 2023Article
- Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.Angewandte Chemie (International ed. in English) · 2022Article
- Recycling Upstream Redox Enzymes Expands the Regioselectivity of Cycloaddition in Pseudo-Aspidosperma Alkaloid Biosynthesis.Journal of the American Chemical Society · 2022Article
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10 authors.
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Abstract
Medium-chain alcohol dehydrogenases (ADHs) comprise a highly conserved enzyme family that catalyse the reversible reduction of aldehydes. However, recent discoveries in plant natural product biosynthesis suggest that the catalytic repertoire of ADHs has been expanded. Here we report the crystal structure of dihydroprecondylocarpine acetate synthase (DPAS), an ADH that catalyses the non-canonical 1,4-reduction of an α,β-unsaturated iminium moiety. Comparison with structures of plant-derived ADHs suggest the 1,4-iminium reduction does not require a proton relay or the presence of a catalytic zinc ion in contrast to canonical 1,2-aldehyde reducing ADHs that require the catalytic zinc and a proton relay. Furthermore, ADHs that catalysed 1,2-iminium reduction required the presence of the catalytic zinc and the loss of the proton relay. This suggests how the ADH active site can be modified to perform atypical carbonyl reductions, providing insight into how chemical reactions are diversified in plant metabolism.
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