The structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition

被引:0
|
作者
Fage C.D. [1 ]
Isiorho E.A. [1 ]
Liu Y. [2 ]
Wagner D.T. [1 ]
Liu H.-W. [2 ,3 ]
Keatinge-Clay A.T. [1 ,3 ]
机构
[1] Department of Molecular Biosciences, University of Texas at Austin, Austin, TX
[2] Division of Medicinal Chemistry, College of Pharmacy, University of Texas at Austin, Austin, TX
[3] Department of Chemistry, University of Texas at Austin, Austin, TX
基金
美国国家卫生研究院;
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D O I
10.1038/nchembio.1768
中图分类号
学科分类号
摘要
In the biosynthetic pathway of the spinosyn insecticides, the tailoring enzyme SpnF performs a [4 + 2] cycloaddition on a 22-membered macrolactone to forge an embedded cyclohexene ring. To learn more about this reaction, which could potentially proceed through a Diels-Alder mechanism, we determined the 1.50-Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization. © 2015 Elsevier Masson SAS. All rights reserved.
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页码:256 / 258
页数:2
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