A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini

Advances in bioinformatics have enabled the discovery of unique enzymatic reactions, particularly for ribosomally synthesized and post-translationally modified peptides (RiPPs). The recently discovered daptides, peptides with their C-terminus replaced by an amine, represent one such case, but the di...

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Tác giả chính:	Shravan R. Dommaraju (22281579) (author)
Tác giả khác:	Sanath K. Kandy (22281582) (author), Hengqian Ren (5759555) (author), Dominic P. Luciano (22281585) (author), Shogo Fujiki (10692093) (author), David Sarlah (1617298) (author), Huimin Zhao (11441) (author), Jonathan R. Chekan (517902) (author), Douglas A. Mitchell (1314975) (author)
Được phát hành:	2025
Những chủ đề:	Biophysics Biochemistry Microbiology Genetics Biotechnology Immunology Infectious Diseases Space Science Astronomical and Space Sciences not elsewhere classified Chemical Sciences not elsewhere classified ycao enzymes convert successive oxidative decarboxylation recently discovered daptides broad substrate tolerance unique enzymatic reactions reconstituted daptide biosynthesis daptide biosynthesis remain thermobifida fusca </ streptomyces azureus </ translationally modified peptides native core peptides versatile enzymatic pathway secondary amine intermediate install new c daptide pathway vivo </ vitro </ n </ enzymatic requirements various peptide terminus replaced terminal imidazoline tailoring family studies showed ripps ). ribosomally synthesized represent one protein substrates leader peptide engineering potential compatible aminoacetone >- dimethylation
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A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini

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