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The Crystal Structure of AbsH3: a Putative FAD-dependent Reductase in the Abyssomicin Biosynthesis Pathway.
Proteins: Structure, Function, and Bioinformatics ( IF 2.9 ) Pub Date : 2020-08-27 , DOI: 10.1002/prot.25994
Jonathan A Clinger 1 , Xiachang Wang 2, 3 , Wenlong Cai 4 , Yanyan Zhu 3, 4 , Mitchell D Miller 1 , Chang-Guo Zhan 3, 4 , Steven G Van Lanen 4 , Jon S Thorson 3, 4 , George N Phillips 1, 5
Affiliation  

Natural products and natural product‐derived compounds have been widely used for pharmaceuticals for many years, and the search for new natural products that may have interesting activity is ongoing. Abyssomicins are natural product molecules that have antibiotic activity via inhibition of the folate synthesis pathway in microbiota. These compounds also appear to undergo a required [4 + 2] cycloaddition in their biosynthetic pathway. Here we report the structure of an flavin adenine dinucleotide‐dependent reductase, AbsH3, from the biosynthetic gene cluster of novel abyssomicins found in Streptomyces sp. LC‐6‐2.

中文翻译:

AbsH3 的晶体结构:Abysomicin 生物合成途径中推定的 FAD 依赖性还原酶。

多年来,天然产物和天然产物衍生化合物已广泛用于药物,并且正在寻找可能具有有趣活性的新天然产物。Abyssomicins 是天然产物分子,通过抑制微生物群中的叶酸合成途径具有抗生素活性。这些化合物似乎也在其生物合成途径中经历了所需的 [4 + 2] 环加成反应。在这里,我们报告了黄素腺嘌呤二核苷酸依赖性还原酶 AbsH3 的结构,该酶来自链霉菌属中发现的新型 abyssomicins 的生物合成基因簇。LC-6-2。
更新日期:2020-08-27
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