Exploring Fluorinase Substrate Tolerance at C-2 of SAM.

IF 2.6 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

ChemBioChem Pub Date : 2024-11-17 DOI:10.1002/cbic.202400861

Phillip T Lowe, Isabeau T Lüddecke, David O'Hagan

引用次数: 0

Abstract

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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探索 SAM C-2 的氟化酶底物耐受性。

通过在腺嘌呤环的 C-2 处引入未经测试的取代基，探索了氟化酶（EC 2.5.1.63）对底物的耐受性。最有活性的类似物是 N-烷基化胺，作为一个类别，它们比 O-或 S-醚好得多。这些结果都得到了硅学分析的支持。这种耐受性拓宽了氟化酶的用途，可将氟-18 同位素引入正电子发射断层扫描应用的配体中。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

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).