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Characterization of the Actinonin Biosynthetic Gene Cluster

Characterization of the Actinonin Biosynthetic Gene Cluster

Felix Wolf, Franziska Leipoldt, Andreas Kulik, Daniel Wibberg, Jörn Kalinowski, Leonard Kaysser

Chembiochem. 2018 Mar 30.

PMID: 29600569

Abstract:

The hydroxamate moiety of the natural product actinonin mediates inhibition of metalloproteinases because of its chelating properties towards divalent cations in the active site of those enzymes. Owing to its antimicrobial activity, actinonin has served as a lead compound for the development of new antibiotic drug candidates. Recently, we identified a putative gene cluster for the biosynthesis of actinonin. Here, we confirm and characterize this cluster by heterologous pathway expression and gene-deletion experiments. We assigned the biosynthetic gene cluster to actinonin production and determine the cluster boundaries. Furthermore, we establish that ActI, an AurF-like oxygenase, is responsible for the N-hydroxylation reaction that forms the hydroxamate warhead. Our findings provide the basis for more detailed investigations of actinonin biosynthesis.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP13434134	Actinonin		13434-13-4	Price

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