A Cupin Epoxidase Catalyzes Epoxycyclohexenone Formation in Fungal Meroterpenoid Biosynthesis

IF 5 1区 化学 Q1 CHEMISTRY, ORGANIC
Yun-Tao Jiang, Xiao-Jun Li, Wu-Xia Xi, Lian-Qiong Du, Yu-Kai Suo, Xu-Ping Zhang, Ping Zhao* and Wei-Guang Wang*, 
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引用次数: 0

Abstract

We identified the par biosynthetic gene cluster from Paraphaeosphaeria sp. C-XB-J-1, responsible for producing epoxycyclohexenone (ECH)-containing meroterpenoids, paraphaeones. In vitro reconstitution revealed the sequential action of the cupin-domain protein ParE and the SDR enzyme ParD in ECH formation. Molecular dynamics analysis and site-directed mutagenesis confirmed critical catalytic residues. This work provides the biochemical evidence for a fungal cupin epoxidase involved in ECH biosynthesis and expands the enzymology of fungal meroterpenoid.

Abstract Image

Abstract Image

一种Cupin环氧化酶在真菌类美罗萜类生物合成中催化环氧环己酮的形成
我们从Paraphaeosphaeria sp. C-XB-J-1中鉴定出了一个paraphasphaeria sp. C-XB-J-1生物合成基因簇,该基因簇负责产生含环氧环己酮(ECH)的巯基萜类化合物paraphaeones。体外重构揭示了铜结构域蛋白ParE和SDR酶ParD在ECH形成中的顺序作用。分子动力学分析和定点诱变证实了关键的催化残基。本研究为真菌铜素环氧化酶参与ECH生物合成提供了生物化学证据,拓展了真菌类美罗萜类化合物的酶学研究。
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来源期刊
Organic Letters
Organic Letters 化学-有机化学
CiteScore
9.30
自引率
11.50%
发文量
1607
审稿时长
1.5 months
期刊介绍: Organic Letters invites original reports of fundamental research in all branches of the theory and practice of organic, physical organic, organometallic,medicinal, and bioorganic chemistry. Organic Letters provides rapid disclosure of the key elements of significant studies that are of interest to a large portion of the organic community. In selecting manuscripts for publication, the Editors place emphasis on the originality, quality and wide interest of the work. Authors should provide enough background information to place the new disclosure in context and to justify the rapid publication format. Back-to-back Letters will be considered. Full details should be reserved for an Article, which should appear in due course.
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