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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.

SUBMITTER: Fage CD

PROVIDER: S-EPMC4366278 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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

Fage Christopher D CD Isiorho Eta A EA Liu Yungnan Y Wagner Drew T DT Liu Hung-wen HW Keatinge-Clay Adrian T AT

Nature chemical biology 20150302 4

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-medi ...[more]

PMID: 25730549

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