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Title: Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering

Abstract

Fatty acids are primary metabolites synthesized by complex, elegant, and essential biosynthetic machinery. Fatty acid synthases resemble an iterative assembly line, with an acyl carrier protein conveying the growing fatty acid to necessary enzymatic domains for modification. Each catalytic domain is a unique enzyme spanning a wide range of folds and structures. Although they harbor the same enzymatic activities, two different types of fatty acid synthase architectures are observed in nature. During recent years, strained petroleum supplies have driven interest in engineering organisms to either produce more fatty acids or specific high value products. Such efforts require a fundamental understanding of the enzymatic activities and regulation of fatty acid synthases. Despite more than one hundred years of research, we continue to learn new lessons about fatty acid synthases' many intricate structural and regulatory elements. Lastly, in this review, we summarize each enzymatic domain and discuss efforts to engineer fatty acid synthases, providing some clues to important challenges and opportunities in the field.

Authors:
 [1];  [1];  [1]
  1. Univ. of California San Diego, La Jolla, CA (United States)
Publication Date:
Research Org.:
Univ. of California, San Diego, CA (United States)
Sponsoring Org.:
USDOE Advanced Research Projects Agency - Energy (ARPA-E)
OSTI Identifier:
1346967
Grant/Contract Number:  
EE0003373
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Molecular BioSystems
Additional Journal Information:
Journal Volume: 11; Journal Issue: 1; Journal ID: ISSN 1742-206X
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Beld, Joris, Lee, D. John, and Burkart, Michael D. Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering. United States: N. p., 2014. Web. doi:10.1039/c4mb00443d.
Beld, Joris, Lee, D. John, & Burkart, Michael D. Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering. United States. doi:10.1039/c4mb00443d.
Beld, Joris, Lee, D. John, and Burkart, Michael D. Mon . "Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering". United States. doi:10.1039/c4mb00443d. https://www.osti.gov/servlets/purl/1346967.
@article{osti_1346967,
title = {Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering},
author = {Beld, Joris and Lee, D. John and Burkart, Michael D.},
abstractNote = {Fatty acids are primary metabolites synthesized by complex, elegant, and essential biosynthetic machinery. Fatty acid synthases resemble an iterative assembly line, with an acyl carrier protein conveying the growing fatty acid to necessary enzymatic domains for modification. Each catalytic domain is a unique enzyme spanning a wide range of folds and structures. Although they harbor the same enzymatic activities, two different types of fatty acid synthase architectures are observed in nature. During recent years, strained petroleum supplies have driven interest in engineering organisms to either produce more fatty acids or specific high value products. Such efforts require a fundamental understanding of the enzymatic activities and regulation of fatty acid synthases. Despite more than one hundred years of research, we continue to learn new lessons about fatty acid synthases' many intricate structural and regulatory elements. Lastly, in this review, we summarize each enzymatic domain and discuss efforts to engineer fatty acid synthases, providing some clues to important challenges and opportunities in the field.},
doi = {10.1039/c4mb00443d},
journal = {Molecular BioSystems},
number = 1,
volume = 11,
place = {United States},
year = {Mon Oct 20 00:00:00 EDT 2014},
month = {Mon Oct 20 00:00:00 EDT 2014}
}

Journal Article:
Free Publicly Available Full Text
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Cited by: 26 works
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