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

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, the 1.50 Å-resol...

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Autores principales: Fage, Christopher D., Isiorho, Eta A., Liu, Yungnan, Wagner, Drew T., Liu, Hung-wen, Keatinge-Clay, Adrian T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4366278/
https://www.ncbi.nlm.nih.gov/pubmed/25730549
http://dx.doi.org/10.1038/nchembio.1768
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author Fage, Christopher D.
Isiorho, Eta A.
Liu, Yungnan
Wagner, Drew T.
Liu, Hung-wen
Keatinge-Clay, Adrian T.
author_facet Fage, Christopher D.
Isiorho, Eta A.
Liu, Yungnan
Wagner, Drew T.
Liu, Hung-wen
Keatinge-Clay, Adrian T.
author_sort Fage, Christopher D.
collection PubMed
description 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, the 1.50 Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine (SAH) was determined. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.
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spelling pubmed-43662782015-10-01 The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition Fage, Christopher D. Isiorho, Eta A. Liu, Yungnan Wagner, Drew T. Liu, Hung-wen Keatinge-Clay, Adrian T. Nat Chem Biol Article 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, the 1.50 Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine (SAH) was determined. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization. 2015-03-02 2015-04 /pmc/articles/PMC4366278/ /pubmed/25730549 http://dx.doi.org/10.1038/nchembio.1768 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Fage, Christopher D.
Isiorho, Eta A.
Liu, Yungnan
Wagner, Drew T.
Liu, Hung-wen
Keatinge-Clay, Adrian T.
The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title_full The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title_fullStr The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title_full_unstemmed The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title_short The Structure of SpnF, a Standalone Enzyme that Catalyzes [4+2] Cycloaddition
title_sort structure of spnf, a standalone enzyme that catalyzes [4+2] cycloaddition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4366278/
https://www.ncbi.nlm.nih.gov/pubmed/25730549
http://dx.doi.org/10.1038/nchembio.1768
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