{"title":"一种可点击的辅酶 A 衍生物探针,用于研究天然产物生物合成过程中磷酸泛乙烯基转移酶的活性。","authors":"Zhiyong Yin , Houchao Xu , Jeroen S. Dickschat","doi":"10.1039/d4ob01485e","DOIUrl":null,"url":null,"abstract":"<div><div>Phosphopantetheinyl transferases activate carrier proteins through attachment of a coenzyme A derived phosphopantetheinyl linker. This study describes a method to monitor this process through a modified HSCoA with an alkyne group, allowing for the Cu-catalysed alkyne–azide cycloaddition of a fluorescent tag. Application of the method in an enzyme screening resulted in the identification of new promiscuous PPTases.</div></div>","PeriodicalId":96,"journal":{"name":"Organic & Biomolecular Chemistry","volume":"22 44","pages":"Pages 8714-8719"},"PeriodicalIF":2.7000,"publicationDate":"2024-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A clickable coenzyme A derived probe for investigating phosphopantetheinyl transferase activity in natural product biosynthesis†\",\"authors\":\"Zhiyong Yin , Houchao Xu , Jeroen S. Dickschat\",\"doi\":\"10.1039/d4ob01485e\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Phosphopantetheinyl transferases activate carrier proteins through attachment of a coenzyme A derived phosphopantetheinyl linker. This study describes a method to monitor this process through a modified HSCoA with an alkyne group, allowing for the Cu-catalysed alkyne–azide cycloaddition of a fluorescent tag. Application of the method in an enzyme screening resulted in the identification of new promiscuous PPTases.</div></div>\",\"PeriodicalId\":96,\"journal\":{\"name\":\"Organic & Biomolecular Chemistry\",\"volume\":\"22 44\",\"pages\":\"Pages 8714-8719\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2024-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Organic & Biomolecular Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/org/science/article/pii/S1477052024008978\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/10/7 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, ORGANIC\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Organic & Biomolecular Chemistry","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/org/science/article/pii/S1477052024008978","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/10/7 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"CHEMISTRY, ORGANIC","Score":null,"Total":0}
引用次数: 0
摘要
磷酸泛硫乙烯基转移酶通过连接辅酶 A 衍生的磷酸泛硫乙烯基连接体来激活载体蛋白。本研究介绍了一种通过带有炔基的改性 HSCoA 监控这一过程的方法,该方法允许铜催化的炔吖啶环加成荧光标签。在酶筛选中应用这种方法,发现了新的杂合 PPT 酶。
A clickable coenzyme A derived probe for investigating phosphopantetheinyl transferase activity in natural product biosynthesis†
Phosphopantetheinyl transferases activate carrier proteins through attachment of a coenzyme A derived phosphopantetheinyl linker. This study describes a method to monitor this process through a modified HSCoA with an alkyne group, allowing for the Cu-catalysed alkyne–azide cycloaddition of a fluorescent tag. Application of the method in an enzyme screening resulted in the identification of new promiscuous PPTases.
期刊介绍:
Organic & Biomolecular Chemistry is an international journal using integrated research in chemistry-organic chemistry. Founded in 2003 by the Royal Society of Chemistry, the journal is published in Semimonthly issues and has been indexed by SCIE, a leading international database. The journal focuses on the key research and cutting-edge progress in the field of chemistry-organic chemistry, publishes and reports the research results in this field in a timely manner, and is committed to becoming a window and platform for rapid academic exchanges among peers in this field. The journal's impact factor in 2023 is 2.9, and its CiteScore is 5.5.