Document Detail


Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities.
MedLine Citation:
PMID:  23248280     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Aliphatic hydrocarbons such as fatty alcohols and petroleum-derived alkanes have numerous applications in the chemical industry. In recent years, the renewable synthesis of aliphatic hydrocarbons has been made possible by engineering microbes to overaccumulate fatty acids. However, to generate end products with the desired physicochemical properties (e.g., fatty aldehydes, alkanes, and alcohols), further conversion of the fatty acid is necessary. A carboxylic acid reductase (CAR) from Mycobacterium marinum was found to convert a wide range of aliphatic fatty acids (C(6)-C(18)) into corresponding aldehydes. Together with the broad-substrate specificity of an aldehyde reductase or an aldehyde decarbonylase, the catalytic conversion of fatty acids to fatty alcohols (C(8)-C(16)) or fatty alkanes (C(7)-C(15)) was reconstituted in vitro. This concept was applied in vivo, in combination with a chain-length-specific thioesterase, to engineer Escherichia coli BL21(DE3) strains that were capable of synthesizing fatty alcohols and alkanes. A fatty alcohol titer exceeding 350 mg·L(-1) was obtained in minimal media supplemented with glucose. Moreover, by combining the CAR-dependent pathway with an exogenous fatty acid-generating lipase, natural oils (coconut oil, palm oil, and algal oil bodies) were enzymatically converted into fatty alcohols across a broad chain-length range (C(8)-C(18)). Together with complementing enzymes, the broad substrate specificity and kinetic characteristics of CAR opens the road for direct and tailored enzyme-catalyzed conversion of lipids into user-ready chemical commodities.
Authors:
M Kalim Akhtar; Nicholas J Turner; Patrik R Jones
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-12-17
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  110     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-03     Completed Date:  2013-02-27     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  87-92     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Food Chemistry, University of Turku, Tykistökatu 6A 6krs, 20520 Turku, Finland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Alkanes / metabolism
Biofuels*
Escherichia coli
Fatty Acids / metabolism*
Fatty Alcohols / metabolism
Kinetics
Mycobacterium marinum / enzymology*
Oxidoreductases / metabolism*
Substrate Specificity
Synthetic Biology / methods*
Chemical
Reg. No./Substance:
0/Alkanes; 0/Biofuels; 0/Fatty Acids; 0/Fatty Alcohols; EC 1.-/Oxidoreductases; EC 1.3.99.-/carboxylic acid reductase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Regulation of the actin-activated MgATPase activity of Acanthamoeba myosin II by phosphorylation of ...
Next Document:  Long-lived microRNA-Argonaute complexes in quiescent cells can be activated to regulate mitogenic re...