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Regioselective Halogenation of Lavanducyanin by a Site-Selective Vanadium-Dependent Chloroperoxidase.

ABSTRACT: Halogenated phenazine meroterpenoids are a structurally unusual family of marine actinobacterial natural products that exhibit antibiotic, antibiofilm, and cytotoxic bioactivities. Despite a lack of established phenazine halogenation biochemistry, genomic analysis of Streptomyces sp. CNZ-289, a prolific lavanducyanin and C2-halogenated derivative producer, suggested the involvement of vanadium-dependent haloperoxidases. We subsequently discovered lavanducyanin halogenase (LvcH), characterized it in vitro as a regioselective vanadium-dependent chloroperoxidase, and applied it in late-stage chemoenzymatic synthesis.

SUBMITTER: Baumgartner JT

PROVIDER: S-EPMC11250029 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature

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Regioselective Halogenation of Lavanducyanin by a Site-Selective Vanadium-Dependent Chloroperoxidase.

Baumgartner Jackson T JT McKinnie Shaun M K SMK

Organic letters 20240627 27

Halogenated phenazine meroterpenoids are a structurally unusual family of marine actinobacterial natural products that exhibit antibiotic, antibiofilm, and cytotoxic bioactivities. Despite a lack of established phenazine halogenation biochemistry, genomic analysis of <i>Streptomyces</i> sp. CNZ-289, a prolific lavanducyanin and C2-halogenated derivative producer, suggested the involvement of vanadium-dependent haloperoxidases. We subsequently discovered lavanducyanin halogenase (LvcH), character ...[more]

PMID: 38934639

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