Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
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- 作者：Dheeraj Khare1 ; Wendi A. Hale2 ; 7 ; Ashootosh Tripathi1 ; Liangcai Gu1 ; 3 ; 8 ; David H. Sherman1 ; 2 ; 3 ; 4 ; William H. Gerwick6 ; Kristina Hå ; kansson2 ; Janet L. Smith1 ; 5 ; janetsmith@umich.edu" class="auth_mail" title="E-mail the corresponding author
- 刊名：Structure
- 出版年：2015
- 出版时间：1 December 2015
- 年：2015
- 卷：23
- 期：12
- 页码：2213-2223
- 全文大小：3223 K
文摘
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An NADPH-dependent cyclopropanase (CurF ER) crystal structure at 0.96 Å is reported
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Two thioester enoyl reductases (JamJ and CurK ERs) are highly similar to CurF ER
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Insertion of a CurF ER “cyclopropanase loop” confers the unusual activity on JamJ ER
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A covalent adduct of NADPH and the enoyl thioester substrate is detected in CurK ER