糖化蛋白的5-硫代组氨酸n -乙酰转移酶。

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2025-06-26 DOI:10.1002/cbic.202400439
Cangsong Liao, David Lim, Gladwin Suryatin Alim, Florian P Seebeck
{"title":"糖化蛋白的5-硫代组氨酸n -乙酰转移酶。","authors":"Cangsong Liao, David Lim, Gladwin Suryatin Alim, Florian P Seebeck","doi":"10.1002/cbic.202400439","DOIUrl":null,"url":null,"abstract":"<p><p>Ovothiol A is a 5-thiohistidine derivative biosynthesized by a broad range of prokaryotic and eukaryotic organisms. Its redox-active mercaptoimidazole side chain is believed to protect cells from oxidative stress. The three enzymes that produce ovothiol A from histidine, cysteine, and S-adenosyl methionine have been identified and characterized. In contrast, no enzymes are known that produce other 5-thiohistidine derivatives. Here, we describe a small family of acetyl-coenzyme A-dependent transferases that produce N-acetyl-5-thiohistidine. The discovery of these enzymes from Proteiniphilum saccharofermentans and related Bacteroidota provides evidence that the 5-thiohistidine class may be structurally and functionally more diverse than previously thought.</p>","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202400439"},"PeriodicalIF":2.6000,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"5-thiohistidine N-acetyltransferase from Proteiniphilum saccharofermentans.\",\"authors\":\"Cangsong Liao, David Lim, Gladwin Suryatin Alim, Florian P Seebeck\",\"doi\":\"10.1002/cbic.202400439\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Ovothiol A is a 5-thiohistidine derivative biosynthesized by a broad range of prokaryotic and eukaryotic organisms. Its redox-active mercaptoimidazole side chain is believed to protect cells from oxidative stress. The three enzymes that produce ovothiol A from histidine, cysteine, and S-adenosyl methionine have been identified and characterized. In contrast, no enzymes are known that produce other 5-thiohistidine derivatives. Here, we describe a small family of acetyl-coenzyme A-dependent transferases that produce N-acetyl-5-thiohistidine. The discovery of these enzymes from Proteiniphilum saccharofermentans and related Bacteroidota provides evidence that the 5-thiohistidine class may be structurally and functionally more diverse than previously thought.</p>\",\"PeriodicalId\":140,\"journal\":{\"name\":\"ChemBioChem\",\"volume\":\" \",\"pages\":\"e202400439\"},\"PeriodicalIF\":2.6000,\"publicationDate\":\"2025-06-26\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ChemBioChem\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1002/cbic.202400439\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemBioChem","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1002/cbic.202400439","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

卵硫醇A是一种由广泛的原核和真核生物合成的5-硫代组氨酸衍生物。其氧化还原活性巯基咪唑侧链被认为可以保护细胞免受氧化应激。从组氨酸、半胱氨酸和s -腺苷蛋氨酸中产生卵硫醇A的三种酶已经被鉴定和表征。相比之下,目前还没有发现能产生其他5-硫代组氨酸衍生物的酶。在这里,我们描述了一个产生n -乙酰-5-硫代组氨酸的乙酰辅酶a依赖性转移酶的小家族。从糖化蛋白菌和相关的拟杆菌门中发现的这些酶提供了证据,证明5-硫代组氨酸类可能在结构和功能上比以前认为的更加多样化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
5-thiohistidine N-acetyltransferase from Proteiniphilum saccharofermentans.

Ovothiol A is a 5-thiohistidine derivative biosynthesized by a broad range of prokaryotic and eukaryotic organisms. Its redox-active mercaptoimidazole side chain is believed to protect cells from oxidative stress. The three enzymes that produce ovothiol A from histidine, cysteine, and S-adenosyl methionine have been identified and characterized. In contrast, no enzymes are known that produce other 5-thiohistidine derivatives. Here, we describe a small family of acetyl-coenzyme A-dependent transferases that produce N-acetyl-5-thiohistidine. The discovery of these enzymes from Proteiniphilum saccharofermentans and related Bacteroidota provides evidence that the 5-thiohistidine class may be structurally and functionally more diverse than previously thought.

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
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
×
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:604180095
Book学术官方微信