The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition

Abstract

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.

DOI: 10.1038/nchembio.1768

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@inproceedings{Fage2015TheSO, title={The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition}, author={Christopher D. Fage and Eta A. Isiorho and Yungnan Liu and Drew T. Wagner and Hung-Wen Liu and Adrian T Keatinge-Clay}, booktitle={Nature chemical biology}, year={2015} }