Peptide biosynthesis is the biological formation and maturation of molecules containing amino-acid residues connected by peptide bonds. Ribosomal pathways translate an encoded precursor sequence, after which biosynthetic enzymes can modify the peptide to establish its mature chemical structure [1]. Leader regions within precursor peptides provide recognition elements that direct modifying enzymes toward the product-forming region [2]. Processing reactions can generate cyclic structures, altered side chains, and other chemical features within ribosomally produced natural peptides [3]. Multiple modifications may occur on a single precursor, including changes in amino-acid stereochemistry and the addition of methyl groups [4]. The mature product thus arises through an ordered relationship between precursor synthesis, enzyme recognition, chemical modification, and release of the processed peptide from any associated precursor regions [1].
- peptide biosynthesis
- precursor peptides
- peptide bonds
- natural products
References
- Maria Papagianni; Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol. Adv. 2003, 21, 465-499, 10.1016/s0734-9750(03)00077-6.
- Jesko Koehnke; Greg Mann; Andrew F Bent; Hannes Ludewig; Sally Shirran; Catherine Botting; Tomas Lebl; Wael E Houssen; Marcel Jaspars; James H Naismith; et al. Structural analysis of leader peptide binding enables leader-free cyanobactin processing. Nat. Chem. Biol. 2015, 11, 558-563, 10.1038/nchembio.1841.
- John A. McIntosh; Mohamed S. Donia; Eric W. Schmidt; Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Nat. Prod. Rep. 2009, 26, 537-559, 10.1039/b714132g.
- Michael F. Freeman; Cristian Gurgui; Maximilian J. Helf; Brandon I. Morinaka; Agustinus R. Uria; Neil J. Oldham; Hans-Georg Sahl; Shigeki Matsunaga; Jörn Piel; Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides. Science 2012, 338, 387-390, 10.1126/science.1226121.