Amino acid tailoring strategies in peptide natural product biosynthesis

非核糖体肽 生物合成 氨基酸 天然产物 肽生物合成 生物化学 生物 肽合成 核糖体RNA 化学 肽序列 计算生物学 定向进化 蛋白质生物合成 合成生物学 核糖体蛋白
作者
Lukas Zimmer,Max Crüsemann
出处
期刊:Trends in chemistry [Elsevier BV]
卷期号:7 (11): 705-718 被引量:1
标识
DOI:10.1016/j.trechm.2025.09.014
摘要

Recently characterized outstanding examples of noncanonical amino acid biosynthesis sequences in modified peptide natural product biosynthetic pathways are reviewed. Enzymatic modifications can occur on single precursors, enzyme-bound intermediates, or post assembly for nonribosomal systems or on precursor peptides for ribosomal systems. Different examples of convergent evolution and cooperation of biosynthetic systems were uncovered. Modified peptide natural products are renowned for their exceptional structural diversity, which translates into a broad spectrum of bioactivities and therapeutic potential. For their biosynthesis, nature has evolved two fundamentally different strategies – through a ribosomal and a nonribosomal route. Pivotal to the peptides’ structural diversity are their underlining amino acid building blocks, often transformed by specialized biosynthetic enzymes into noncanonical residues, frequently crucial for their bioactivities. In this review, we highlight recent advances in deciphering the biosynthesis of unusual and highly modified amino acids across peptide natural product biosynthetic pathways. We introduce different tailoring routes that may lead to similar or even the same products and outline unexpected combinations of pathway types discovered to produce complex chemistry. Modified peptide natural products are renowned for their exceptional structural diversity, which translates into a broad spectrum of bioactivities and therapeutic potential. For their biosynthesis, nature has evolved two fundamentally different strategies – through a ribosomal and a nonribosomal route. Pivotal to the peptides’ structural diversity are their underlining amino acid building blocks, often transformed by specialized biosynthetic enzymes into noncanonical residues, frequently crucial for their bioactivities. In this review, we highlight recent advances in deciphering the biosynthesis of unusual and highly modified amino acids across peptide natural product biosynthetic pathways. We introduce different tailoring routes that may lead to similar or even the same products and outline unexpected combinations of pathway types discovered to produce complex chemistry.
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