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

Christopher D. Fage | Zendy; Eta A. Isiorho | Zendy; Yung-nan Liu | Zendy; Drew T. Wagner | Zendy; Hungwen Liu | Zendy; Adrian T. KeatingeClay | Zendy

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The 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.

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