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  • A biaryl-linked tripeptide from Planomonospora reveals a widespread class of minimal RiPP gene clusters.

A biaryl-linked tripeptide from Planomonospora reveals a widespread class of minimal RiPP gene clusters.

Cell chemical biology (2020-12-16)
Mitja M Zdouc, Mohammad M Alanjary, Guadalupe S Zarazúa, Sonia I Maffioli, Max Crüsemann, Marnix H Medema, Stefano Donadio, Margherita Sosio
초록

Microbial natural products impress by their bioactivity, structural diversity, and ingenious biosynthesis. While screening the less exploited actinobacterial genus Planomonospora, two cyclopeptides were discovered, featuring an unusual Tyr-His biaryl bridging across a tripeptide scaffold, with the sequences N-acetyl-Tyr-Tyr-His and N-acetyl-Tyr-Phe-His. Planomonospora genomes pointed toward a ribosomal synthesis of the cyclopeptide from a pentapeptide precursor encoded by 18-bp bytA, to our knowledge the smallest coding gene ever reported. Closely linked to bytA is bytO, encoding a cytochrome P450 monooxygenase likely responsible for biaryl installment. In Streptomyces, the bytAO segment was sufficient to direct production of the crosslinked N-acetylated Tyr-Tyr-His tripeptide. Bioinformatic analysis of related cytochrome P450 monooxygenases indicated that they constitute a widespread family of enzymes, and the corresponding genes are closely linked to 5-amino acid coding sequences in approximately 200 (actino)bacterial genomes, all with potential for biaryl linkage between amino acids 1 and 3. We propose the named biarylitides this family of RiPPs.

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Sigma-Aldrich
Angiotensin I Converting Enzyme (ACE) Activity Assay Kit (Fluorometric), sufficient for 200 fluorometric tests