Open AccessThe structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition
Author(s) -
Christopher D. Fage,
Eta A. Isiorho,
Yung-Nan Liu,
Drew T. Wagner,
Hungwen Liu,
Adrian T. KeatingeClay
Publication year - 2015
Publication title -
nature chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.412
H-Index - 216
eISSN - 1552-4469
pISSN - 1552-4450
DOI - 10.1038/nchembio.1768
Subject(s) - cycloaddition , chemistry , ring (chemistry) , stereochemistry , enzyme , cyclohexene , biocatalysis , mechanism (biology) , crystal structure , reaction mechanism , catalysis , biochemistry , crystallography , organic chemistry , physics , quantum mechanics
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.