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Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1 -gymA6 in Escherichia coli resulted in the formation of cyclo-l-Tyr-l-Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1 -GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C-C coupling within cyclo-l-Tyr-l-Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine-containing guatyromycines, instead of the reported tryptophan-nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.

Citation

Jing Liu, Lauritz Harken, Yiling Yang, Xiulan Xie, Shu-Ming Li. Widely Distributed Bifunctional Bacterial Cytochrome P450 Enzymes Catalyze both Intramolecular C-C Bond Formation in cyclo-l-Tyr-l-Tyr and Its Coupling with Nucleobases. Angewandte Chemie (International ed. in English). 2022 May 16;61(21):e202200377

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PMID: 35201649

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