The structure of the sidechain crosslinked Tyr‐Leu‐Trp peptide produced by the biarylitide crosslinking cytochrome P450Blt from Micromonospora sp. MW‐13 has been reanalysed by a series of NMR, computational and isotope labelling experiments and shown to contain a C‐N rather than a C‐O bond. Additional in vivo experiments using such a modified peptide show there is a general tolerance of biarylitide crosslinking P450 enzymes for histidine to tryptophan mutations within their minimal peptide substrate sequences despite the lack of such residues noted in natural biarylitide gene clusters. This work further highlights the impressive ability of P450s from biarylitide biosynthesis pathways as biocatalysts for the formation of a range of sidechain crosslinked tripeptides.

中文翻译：

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由二芳基酯交联细胞色素 P450BLT 产生的含色氨酸的环状三肽的结构重新排列

由小单孢菌属的联芳基肽交联细胞色素 P450Blt 产生的侧链交联 Tyr-Leu-Trp 肽的结构。通过一系列核磁共振、计算和同位素标记实验对 MW-13 进行了重新分析，结果表明它含有 C-N 键而不是 C-O 键。使用此类修饰肽的其他体内实验表明，联芳基交联 P450 酶对其最小肽底物序列内的组氨酸至色氨酸突变具有普遍耐受性，尽管天然联芳基基因簇中缺乏此类残基。这项工作进一步强调了联芳基肽生物合成途径中的 P450 作为形成一系列侧链交联三肽的生物催化剂的令人印象深刻的能力。