Suppr超能文献

形成 Diels-Alderase 的十氢化萘的结构多样性。

Structural diversity of decalin forming Diels-Alderase.

机构信息

School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.

出版信息

Biosci Biotechnol Biochem. 2024 Jun 21;88(7):719-726. doi: 10.1093/bbb/zbae040.

Abstract

The Diels-Alder (DA) reaction, specifically referring to the [4 + 2] cycloaddition reaction in pericyclic reactions, is a process that forms two carbon-carbon covalent bonds in a single step via an electron ring transition state. Among the secondary metabolites produced by microorganisms, numerous compounds are biosynthesized through DA reactions, most of which are enzymatic. Our research group has discovered an enzyme named Diels-Alderase (DAase) that catalyzes the DA reaction in filamentous fungi, and we have been investigating its catalytic mechanism. This review describes the reported microbial DAase enzymes, with a particular focus on those involved in the construction of the decalin ring.

摘要

Diels-Alder(DA)反应,特别是在周环反应中的[4+2]环加成反应,是通过电子环过渡态在单个步骤中形成两个碳-碳共价键的过程。在微生物产生的次级代谢产物中,许多化合物通过 DA 反应生物合成,其中大多数是酶促的。我们的研究小组发现了一种在丝状真菌中催化 DA 反应的酶,名为 Diels-Alderase(DAase),并一直在研究其催化机制。本文综述了报道的微生物 DAase 酶,特别关注那些参与构建十氢化萘环的酶。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验