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Title: 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, in this paper we determined the 1.50-Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. Finally, this sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.

Authors:
 [1];  [1];  [2];  [1];  [3];  [4]
  1. Univ. of Texas, Austin, TX (United States). Dept. of Molecular Biosciences
  2. Univ. of Texas, Austin, TX (United States). College of Pharmacy. Division of Medicinal Chemistry
  3. Univ. of Texas, Austin, TX (United States). College of Pharmacy. Division of Medicinal Chemistry. Dept. of Chemistry
  4. Univ. of Texas, Austin, TX (United States). Dept. of Molecular Biosciences. Dept. of Chemistry
Publication Date:
Research Org.:
Univ. of Texas, Austin, TX (United States)
Sponsoring Org.:
USDOE Office of Science (SC); National Inst. of Health (NIH) (United States); Welch Foundation (United States)
OSTI Identifier:
1177446
Grant/Contract Number:
AC02-06CH11357; GM106112; GM035906; GM040541; F-1712; F-1511
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Nature Chemical Biology
Additional Journal Information:
Journal Volume: 11; Journal Issue: 4; Journal ID: ISSN 1552-4450
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; Biochemistry; Biosynthesis; Natural products; X-ray crystallography

Citation Formats

Fage, Christopher D., Isiorho, Eta A., Liu, Yungnan, Wagner, Drew T., Liu, Hung-wen, and Keatinge-Clay, Adrian T. The structure of SpnF a standalone enzyme that catalyzes [4 + 2] cycloaddition. United States: N. p., 2015. Web. doi:10.1038/nchembio.1768.
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. United States. doi:10.1038/nchembio.1768.
Fage, Christopher D., Isiorho, Eta A., Liu, Yungnan, Wagner, Drew T., Liu, Hung-wen, and Keatinge-Clay, Adrian T. Mon . "The structure of SpnF a standalone enzyme that catalyzes [4 + 2] cycloaddition". United States. doi:10.1038/nchembio.1768. https://www.osti.gov/servlets/purl/1177446.
@article{osti_1177446,
title = {The structure of SpnF a standalone enzyme that catalyzes [4 + 2] cycloaddition},
author = {Fage, Christopher D. and Isiorho, Eta A. and Liu, Yungnan and Wagner, Drew T. and Liu, Hung-wen and Keatinge-Clay, Adrian T.},
abstractNote = {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, in this paper we determined the 1.50-Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. Finally, this sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.},
doi = {10.1038/nchembio.1768},
journal = {Nature Chemical Biology},
number = 4,
volume = 11,
place = {United States},
year = {Mon Mar 02 00:00:00 EST 2015},
month = {Mon Mar 02 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
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Cited by: 35 works
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