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Pathway Description
Fatty Acid Oxidation (Butanoate)
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-08-14
Last Updated: 2025-11-10
Fatty acid oxidation is also known as beta-oxidation. Fatty acids are an important energy source because they are anhydrous and can be reduced. Fatty acids are good sources of energy as they yield more energy than carbohydrates. The fatty acid oxidation pathway degrades fatty acids into acetyl-CoA under anaerobic and aerobic conditions. Enzymes of this pathway can process short and long chain fatty acids. The first step in the pathway is the conversion of acyl-CoA to enoyl-CoA. The pathway continues in a cycle, each turn removing two carbon atoms from the input acyl-CoA to produce acetyl-CoA. Each turn also produces NADH.
References
Fatty Acid Oxidation (Butanoate) References
Campbell JW, Morgan-Kiss RM, Cronan JE Jr: A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway. Mol Microbiol. 2003 Feb;47(3):793-805.
Pubmed: 12535077
Clark D: Regulation of fatty acid degradation in Escherichia coli: analysis by operon fusion. J Bacteriol. 1981 Nov;148(2):521-6.
Pubmed: 6271734
Morgan-Kiss RM, Cronan JE: The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase. J Biol Chem. 2004 Sep 3;279(36):37324-33. doi: 10.1074/jbc.M405233200. Epub 2004 Jun 22.
Pubmed: 15213221
Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E: Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. doi: 10.1074/jbc.273.40.25974.
Pubmed: 9748275
Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
Pubmed: 9205837
Yang SY, Yang XY, Healy-Louie G, Schulz H, Elzinga M: Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. J Biol Chem. 1990 Jun 25;265(18):10424-9.
Pubmed: 2191949
Nakahigashi K, Inokuchi H: Nucleotide sequence of the fadA and fadB genes from Escherichia coli. Nucleic Acids Res. 1990 Aug 25;18(16):4937. doi: 10.1093/nar/18.16.4937.
Pubmed: 2204034
DiRusso CC: Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes. J Bacteriol. 1990 Nov;172(11):6459-68. doi: 10.1128/jb.172.11.6459-6468.1990.
Pubmed: 1699931
Ferrandez A, Garcia JL, Diaz E: Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12. J Bacteriol. 1997 Apr;179(8):2573-81. doi: 10.1128/jb.179.8.2573-2581.1997.
Pubmed: 9098055
This pathway was generated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Generated from SMP0000781
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0001033
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