Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering

Beld, Joris; Lee, D. John; Burkart, Michael D.

doi:10.1039/c4mb00443d

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

Journal Article · Mon Oct 20 00:00:00 EDT 2014 · Molecular BioSystems

DOI:https://doi.org/10.1039/c4mb00443d· OSTI ID:1346967

Beld, Joris ^[1]; Lee, D. John ^[1]; Burkart, Michael D. ^[1]

Univ. of California San Diego, La Jolla, CA (United States)

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.

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Research Organization:: Univ. of California, San Diego, CA (United States)

Sponsoring Organization:: USDOE Advanced Research Projects Agency - Energy (ARPA-E)

Grant/Contract Number:: EE0003373

OSTI ID:: 1346967

Journal Information:: Molecular BioSystems, Vol. 11, Issue 1; ISSN 1742-206X

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 122 works

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