{"title":"探索 SAM C-2 的氟化酶底物耐受性。","authors":"Phillip T Lowe, Isabeau T Lüddecke, David O'Hagan","doi":"10.1002/cbic.202400861","DOIUrl":null,"url":null,"abstract":"<p><p>The substrate tolerance of the fluorinase enzyme (EC 2.5.1.63) is explored by introducing untested substituents at C-2 of the adenine ring. The most active analogues were N-alkylated amines and as a class these were much better than O- or S- ethers. The outcomes are supported by in silico analysis. This tolerance broadens the utility of the fluorinase as a tool for introducing the fluorine-18 isotope into ligands for positron emission tomography applications.</p>","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202400861"},"PeriodicalIF":2.6000,"publicationDate":"2024-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring Fluorinase Substrate Tolerance at C-2 of SAM.\",\"authors\":\"Phillip T Lowe, Isabeau T Lüddecke, David O'Hagan\",\"doi\":\"10.1002/cbic.202400861\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The substrate tolerance of the fluorinase enzyme (EC 2.5.1.63) is explored by introducing untested substituents at C-2 of the adenine ring. The most active analogues were N-alkylated amines and as a class these were much better than O- or S- ethers. The outcomes are supported by in silico analysis. This tolerance broadens the utility of the fluorinase as a tool for introducing the fluorine-18 isotope into ligands for positron emission tomography applications.</p>\",\"PeriodicalId\":140,\"journal\":{\"name\":\"ChemBioChem\",\"volume\":\" \",\"pages\":\"e202400861\"},\"PeriodicalIF\":2.6000,\"publicationDate\":\"2024-11-17\",\"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.202400861\",\"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.202400861","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}
Exploring Fluorinase Substrate Tolerance at C-2 of SAM.
The substrate tolerance of the fluorinase enzyme (EC 2.5.1.63) is explored by introducing untested substituents at C-2 of the adenine ring. The most active analogues were N-alkylated amines and as a class these were much better than O- or S- ethers. The outcomes are supported by in silico analysis. This tolerance broadens the utility of the fluorinase as a tool for introducing the fluorine-18 isotope into ligands for positron emission tomography applications.
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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).
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