ArticleMethods in enzymology2024
Vanadium haloperoxidases as noncanonical terpene synthases.
Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Understanding the role of vanadium: insights into bacterial responses and adaptations.Frontiers in microbiology · 2026Review
- Separation of halide oxidation and substrate halogenation chemistries rationalizes site-selective vanadium dependent haloperoxidase catalysis.bioRxiv : the preprint server for biology · 2025Article
- Vanadium-dependent haloperoxidases from diverse microbes halogenate exogenous alkyl quinolone quorum sensing signals.bioRxiv : the preprint server for biology · 2024Article
- Regioselective Halogenation of Lavanducyanin by a Site-Selective Vanadium-Dependent Chloroperoxidase.Organic letters · 2024Article
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5 authors.
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Abstract
Vanadium-dependent haloperoxidases (VHPOs) are a unique family of enzymes that utilize vanadate, an aqueous halide ion, and hydrogen peroxide to produce an electrophilic halogen species that can be incorporated into electron rich organic substrates. This halogen species can react with terpene substrates and trigger halonium-induced cyclization in a manner reminiscent of class II terpene synthases. While not all VHPOs act in this capacity, several notable examples from algal and actinobacterial species have been characterized to catalyze regio- and enantioselective reactions on terpene and meroterpenoid substrates, resulting in complex halogenated cyclic terpenes through the action of single enzyme. In this article, we describe the expression, purification, and chemical assays of NapH4, a difficult to express characterized VHPO that catalyzes the chloronium-induced cyclization of its meroterpenoid substrate.
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