ArticleAngewandte Chemie (International ed. in English)2023
Actinorhodin Biosynthesis Terminates with an Unprecedented Biaryl Coupling Reaction.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Pd(II)-Catalyzed C-H Activation/ACS omega · 2026Article
- Construction and Diversification of Natural Product Biosynthetic Gene Clusters at High Efficiency and Accuracy.ACS synthetic biology · 2025Article
- Mapping epoxyquinoid biosynthesis: Enzyme functions across bacteria and fungi.Journal of industrial microbiology & biotechnology · 2024Review
- Recent advances in enzymatic carbon-carbon bond formation.RSC advances · 2024Review
- Di-Isatropolone C, a Spontaneous Isatropolone C Dimer Derivative with Autophagy Activity.Molecules (Basel, Switzerland) · 2024Article
- Actinorhodin Biosynthesis Terminates with an Unprecedented Biaryl Coupling Reaction.Angewandte Chemie (International ed. in English) · 2023Article
- Co-factor independent oxidases ncnN and actVA-3 are involved in the dimerization of benzoisochromanequinone antibiotics in naphthocyclinone and actinorhodin biosynthesis.FEMS microbiology letters · 2023Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A plethora of dimeric natural products exist with diverse chemical structures and biological activities. A major strategy for dimerization is aryl coupling catalyzed by cytochrome P450 or laccase. Actinorhodin (ACT) from Streptomyces coelicolor A3(2) has a dimeric pyranonaphthoquinone structure connected by a C-C bond. In this study, we identified an NmrA-family dimerizing enzyme, ActVA-ORF4, and a cofactor-independent oxidase, ActVA-ORF3, both involved in the last step of ACT biosynthesis. ActVA-ORF4 is a unique NAD(P)H-dependent enzyme that catalyzes the intermolecular C-C bond formation using 8-hydroxydihydrokalafungin (DHK-OH) as the sole substrate. On the other hand, ActVA-ORF3 was found to be a quinone-forming enzyme that produces the coupling substrate, DHK-OH and the final product, ACT. Consequently, the functional assignment of all essential enzymes in the biosynthesis of ACT, one of the best-known model natural products, has been completed.
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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.