ArticlePlanta2021
A cytochrome P450 CYP81AM1 from Tripterygium wilfordii catalyses the C-15 hydroxylation of dehydroabietic acid.
Article in Planta, 2021. 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, 16 citations in OpenAlex.
- Cross-stage single-cell and spatial metabolome analyses reveal periderm specialization and tanshinone biosynthesis in Salvia miltiorrhiza roots.The New phytologist · 2026Article
- A Review of Plant-Derived Diterpenoid Biosynthesis: From Structural Scaffold Diversity and Lineage-Associated Distribution to Enzyme Mining and Discovery Strategies.Molecules (Basel, Switzerland) · 2026Review
- CYP72D19 from Tripterygium wilfordii catalyzes C-2 hydroxylation of abietane-type diterpenoids.Plant cell reports · 2023Article
- Uncovering a miltiradiene biosynthetic gene cluster in the Lamiaceae reveals a dynamic evolutionary trajectory.Nature communications · 2023Article
- Functional Characterization of a 2OGD Involved in Abietane-Type Diterpenoids Biosynthetic Pathway inFrontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
MAIN
conclusionA novel cytochrome P450 from Tripterygium wilfordii, CYP81AM1, specifically catalyses the C-15 hydroxylation of dehydroabietic acid. This is the first CYP450 to be found in plants with this function. Cytochrome P450 oxygenases (CYPs) play an important role in the post-modification in biosynthesis of plant bioactive terpenoids. Here, we found that CYP81AM1 can catalyze the formation of 15-hydroxydehydroabietic acid by in vitro enzymatic reactions and in vivo yeast feeding assays. This is the first study to show that CYP81 family enzymes are involved in the hydroxylation of abietane diterpenoids. At the same time, we found that CYP81AM1 could not catalyse abietatriene and dehydroabietinol, suggesting that the occurrence of the reaction may be related to the carboxyl group. Through molecular docking and site mutations, it was found that some amino acid sites (F104, K107) near the carboxyl group had an important effect on enzyme activity, also suggesting that the carboxyl group played an important role in the occurrence of the reaction.
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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.