{"title":"atp依赖性合成酶的酶促叠氮化物合成","authors":"Yohei Katsuyama","doi":"10.1016/j.checat.2024.101226","DOIUrl":null,"url":null,"abstract":"In a recent issue of <em>Nature Chemistry</em>, Zhang and coworkers showed that the ATP-dependent <em>N</em>-nitrosylase Tri17 can catalyze azide synthesis. Tri17 is a promiscuous enzyme that can catalyze <em>N</em>-nitrosylation of various substrates. When specific substrates were used, it also catalyzed the dehydration of the <em>N</em>-nitroso moiety to synthesize an azide moiety.","PeriodicalId":53121,"journal":{"name":"Chem Catalysis","volume":"12 1","pages":""},"PeriodicalIF":11.5000,"publicationDate":"2024-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Enzymatic azide synthesis by ATP-dependent synthetase\",\"authors\":\"Yohei Katsuyama\",\"doi\":\"10.1016/j.checat.2024.101226\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In a recent issue of <em>Nature Chemistry</em>, Zhang and coworkers showed that the ATP-dependent <em>N</em>-nitrosylase Tri17 can catalyze azide synthesis. Tri17 is a promiscuous enzyme that can catalyze <em>N</em>-nitrosylation of various substrates. When specific substrates were used, it also catalyzed the dehydration of the <em>N</em>-nitroso moiety to synthesize an azide moiety.\",\"PeriodicalId\":53121,\"journal\":{\"name\":\"Chem Catalysis\",\"volume\":\"12 1\",\"pages\":\"\"},\"PeriodicalIF\":11.5000,\"publicationDate\":\"2024-12-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chem Catalysis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/j.checat.2024.101226\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chem Catalysis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/j.checat.2024.101226","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Enzymatic azide synthesis by ATP-dependent synthetase
In a recent issue of Nature Chemistry, Zhang and coworkers showed that the ATP-dependent N-nitrosylase Tri17 can catalyze azide synthesis. Tri17 is a promiscuous enzyme that can catalyze N-nitrosylation of various substrates. When specific substrates were used, it also catalyzed the dehydration of the N-nitroso moiety to synthesize an azide moiety.
期刊介绍：
Chem Catalysis is a monthly journal that publishes innovative research on fundamental and applied catalysis, providing a platform for researchers across chemistry, chemical engineering, and related fields. It serves as a premier resource for scientists and engineers in academia and industry, covering heterogeneous, homogeneous, and biocatalysis. Emphasizing transformative methods and technologies, the journal aims to advance understanding, introduce novel catalysts, and connect fundamental insights to real-world applications for societal benefit.
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