An Engineered Biarylitide Cross-Linking P450 from RiPP Biosynthesis Generates Alternative Cyclic Peptides

Cytochrome-P450-mediated cross-linking of ribosomally encoded peptides (RiPPs) is rapidly expanding and displays great potential for biocatalysis. Here, we demonstrate that active site engineering of the biarylitide cross-linking enzyme P450Blt enables the formation of His-X-Tyr and Tyr-X-Tyr cross-...

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Bibliographic Details
Published in:	Organic letters Vol. 26; no. 9; pp. 1828 - 1833
Main Authors:	Treisman, Maxine, Coe, Laura, Zhao, Yongwei, Sasi, Vishnu Mini, Gullick, Jemma, Hansen, Mathias H., Ly, Aviva, Leichthammer, Victor, Hess, Caroline, Machell, Daniel L., Schittenhelm, Ralf B., Hooper, Joel, Jackson, Colin J., Tailhades, Julien, De Voss, James J., Cryle, Max J.
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 08-03-2024
Subjects:	Biocatalysis Catalytic Domain Cytochrome P-450 Enzyme System Peptides - chemistry Peptides, Cyclic - metabolism
Online Access:	Get full text
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Summary:	Cytochrome-P450-mediated cross-linking of ribosomally encoded peptides (RiPPs) is rapidly expanding and displays great potential for biocatalysis. Here, we demonstrate that active site engineering of the biarylitide cross-linking enzyme P450Blt enables the formation of His-X-Tyr and Tyr-X-Tyr cross-linked peptides, thus showing how such P450s can be further exploited to produce alternate cyclic tripeptides with controlled cross-linking states.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1523-7060 1523-7052
DOI:	10.1021/acs.orglett.3c04366