Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Fatty Acid Oxidation
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-01-25
Last Updated: 2024-12-05
Fatty acid oxidation is also known as beta-oxidation. The fatty acid oxidation pathway converts fatty acids into acetyl-CoA under both anaerobic and aerobic conditions. Enzymes in this pathway can process short and long chain fatty acids, both starting 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 and NADH. Fatty acids are an important source of energy because they can be reduced due to their anhydrous properties. In addition, fatty acid oxidation yields more energy when compared to carbohydrates.
References
Fatty Acid Oxidation 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
Doi H, Hoshino Y, Nakase K, Usuda Y: Reduction of hydrogen peroxide stress derived from fatty acid beta-oxidation improves fatty acid utilization in Escherichia coli. Appl Microbiol Biotechnol. 2014 Jan;98(2):629-39. doi: 10.1007/s00253-013-5327-6. Epub 2013 Oct 30.
Pubmed: 24169950
Black PN, DiRusso CC, Metzger AK, Heimert TL: Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J Biol Chem. 1992 Dec 15;267(35):25513-20.
Pubmed: 1460045
Fulda M, Heinz E, Wolter FP: The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family. Mol Gen Genet. 1994 Feb;242(3):241-9. doi: 10.1007/bf00280412.
Pubmed: 8107670
Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, 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, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. doi: 10.1093/dnares/3.6.379.
Pubmed: 9097040
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
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
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
Touchon M, Hoede C, Tenaillon O, Barbe V, Baeriswyl S, Bidet P, Bingen E, Bonacorsi S, Bouchier C, Bouvet O, Calteau A, Chiapello H, Clermont O, Cruveiller S, Danchin A, Diard M, Dossat C, Karoui ME, Frapy E, Garry L, Ghigo JM, Gilles AM, Johnson J, Le Bouguenec C, Lescat M, Mangenot S, Martinez-Jehanne V, Matic I, Nassif X, Oztas S, Petit MA, Pichon C, Rouy Z, Ruf CS, Schneider D, Tourret J, Vacherie B, Vallenet D, Medigue C, Rocha EP, Denamur E: Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths. PLoS Genet. 2009 Jan;5(1):e1000344. doi: 10.1371/journal.pgen.1000344. Epub 2009 Jan 23.
Pubmed: 19165319
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 SMP0000781
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Settings