| Autor: |
Liu, Jing, Liu, Runze, He, Bei-Bei, Lin, Xiaoqian, Guo, Longcheng, Wu, Gengfan, Li, Yong-Xin |
| Zdroj: |
ACS Bio & Med Chem Au; December 2024, Vol. 4 Issue: 6 p268-279, 12p |
| Abstrakt: |
Macrocyclization is a vital process in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), significantly enhancing their structural diversity and biological activity. Universally found in living organisms, cytochrome P450 enzymes (P450s) are versatile catalysts that facilitate a wide array of chemical transformations and have recently been discovered to contribute to the expansion and complexity of the chemical spectrum of RiPPs. Particularly, P450-catalyzed biaryl-bridged RiPPs, characterized by highly modified structures, represent an intriguing but underexplored class of natural products, as demonstrated by the recent discovery of tryptorubin A, biarylitide and cittilin. These P450 enzymes demonstrate their versatility by facilitating peptide macrocyclization through the formation of carbon–carbon (C–C), carbon–nitrogen (C–N) and ether bonds between the side chains of tyrosine (Tyr), tryptophan (Trp) and histidine (His). This Review briefly highlights the latest progress in P450-catalyzed macrocyclization within RiPP biosynthesis, resulting in the generation of structurally complex RiPPs. These findings have expedited the discovery and detailed analysis of new P450s engaged in RiPP biosynthetic pathways. |
| Databáze: |
Supplemental Index |
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