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

March 2nd, 2015 by Christopher D Fage

Nature Chemical Biology 11, 256 (2015). doi:10.1038/nchembio.1768

Authors: Christopher D Fage, Eta A Isiorho, Yungnan Liu, Drew T Wagner, Hung-wen Liu & Adrian T Keatinge-Clay

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.

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