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

IF 6.9 2区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Current Opinion in Chemical Biology Pub Date : 2024-05-20 DOI:10.1016/j.cbpa.2024.102467
Jeff Y. Chen, Wilfred A. van der Donk
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Abstract

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.

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参与异常肽修饰的多核非血红素铁依赖性氧化酶(MNIOs)
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。
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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.
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