参与异常肽修饰的多核非血红素铁依赖性氧化酶(MNIOs)

IF 6.9 2区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Jeff Y. Chen, Wilfred A. van der Donk
{"title":"参与异常肽修饰的多核非血红素铁依赖性氧化酶(MNIOs)","authors":"Jeff Y. Chen,&nbsp;Wilfred A. van der Donk","doi":"10.1016/j.cbpa.2024.102467","DOIUrl":null,"url":null,"abstract":"<div><p>Multinuclear non-heme iron dependent oxidative enzymes (MNIOs), formerly known as domain of unknown function 692 (DUF692), are involved in the post-translational modification of peptides during the biosynthesis of peptide-based natural products. These enzymes catalyze highly unusual and diverse chemical modifications. Several class-defining features of this large family (&gt;14 000 members) are beginning to emerge. Structurally, the enzymes are characterized by a TIM-barrel fold and a set of conserved residues for a di- or tri–iron binding site. They use molecular oxygen to modify peptide substrates, often in a four-electron oxidation taking place at a cysteine residue. This review summarizes the current understanding of MNIOs. Four modifications are discussed in detail: oxazolone-thioamide formation, β-carbon excision, hydantoin-macrocycle formation, and 5-thiooxazole formation. Briefly discussed are two other reactions that do not take place on Cys residues.</p></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"80 ","pages":"Article 102467"},"PeriodicalIF":6.9000,"publicationDate":"2024-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1367593124000437/pdfft?md5=ff0d2067bb16ebe523993dbaeab8b350&pid=1-s2.0-S1367593124000437-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications\",\"authors\":\"Jeff Y. Chen,&nbsp;Wilfred A. van der Donk\",\"doi\":\"10.1016/j.cbpa.2024.102467\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Multinuclear non-heme iron dependent oxidative enzymes (MNIOs), formerly known as domain of unknown function 692 (DUF692), are involved in the post-translational modification of peptides during the biosynthesis of peptide-based natural products. These enzymes catalyze highly unusual and diverse chemical modifications. Several class-defining features of this large family (&gt;14 000 members) are beginning to emerge. Structurally, the enzymes are characterized by a TIM-barrel fold and a set of conserved residues for a di- or tri–iron binding site. They use molecular oxygen to modify peptide substrates, often in a four-electron oxidation taking place at a cysteine residue. This review summarizes the current understanding of MNIOs. Four modifications are discussed in detail: oxazolone-thioamide formation, β-carbon excision, hydantoin-macrocycle formation, and 5-thiooxazole formation. Briefly discussed are two other reactions that do not take place on Cys residues.</p></div>\",\"PeriodicalId\":291,\"journal\":{\"name\":\"Current Opinion in Chemical Biology\",\"volume\":\"80 \",\"pages\":\"Article 102467\"},\"PeriodicalIF\":6.9000,\"publicationDate\":\"2024-05-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S1367593124000437/pdfft?md5=ff0d2067bb16ebe523993dbaeab8b350&pid=1-s2.0-S1367593124000437-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Opinion in Chemical Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1367593124000437\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Opinion in Chemical Biology","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1367593124000437","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

多核非血红素铁依赖性氧化酶(MNIOs),以前称为未知功能域 692(DUF692),在以肽为基础的天然产品的生物合成过程中参与肽的翻译后修饰。这些酶催化了非常不寻常和多样化的化学修饰。这个庞大家族(共有 14 000 个成员)的几个类定义特征已开始显现。从结构上看,这些酶的特点是具有 TIM 桶状折叠结构和一组用于二铁或三铁结合位点的保守残基。它们利用分子氧修饰肽底物,通常是在半胱氨酸残基上进行四电子氧化。本综述总结了目前对 MNIOs 的了解。其中详细讨论了四种修饰反应:恶唑酮-硫代酰胺形成、β-碳切除、海因-大环形成和 5-硫恶唑形成。还简要讨论了不在 Cys 残基上发生的另外两种反应。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications

Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications

Multinuclear non-heme iron dependent oxidative enzymes (MNIOs), formerly known as domain of unknown function 692 (DUF692), are involved in the post-translational modification of peptides during the biosynthesis of peptide-based natural products. These enzymes catalyze highly unusual and diverse chemical modifications. Several class-defining features of this large family (>14 000 members) are beginning to emerge. Structurally, the enzymes are characterized by a TIM-barrel fold and a set of conserved residues for a di- or tri–iron binding site. They use molecular oxygen to modify peptide substrates, often in a four-electron oxidation taking place at a cysteine residue. This review summarizes the current understanding of MNIOs. Four modifications are discussed in detail: oxazolone-thioamide formation, β-carbon excision, hydantoin-macrocycle formation, and 5-thiooxazole formation. Briefly discussed are two other reactions that do not take place on Cys residues.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Current Opinion in Chemical Biology
Current Opinion in Chemical Biology 生物-生化与分子生物学
CiteScore
13.30
自引率
1.30%
发文量
113
审稿时长
74 days
期刊介绍: COCHBI (Current Opinion in Chemical Biology) is a systematic review journal designed to offer specialists a unique and educational platform. Its goal is to help professionals stay informed about the growing volume of information in the field of Chemical Biology through systematic reviews.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信