Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: fatty acid β-oxidation II (plants)
|Superclasses:||Degradation/Utilization/Assimilation → Fatty Acid and Lipids Degradation → Fatty Acids Degradation|
Expected Taxonomic Range: Viridiplantae
The major site for fatty acid β-oxidation in animal cells is the mitochondrion, although partial β-oxidation has also been shown to occur in peroxisomes (see pathway fatty acid β-oxidation VI (peroxisome)) (reviewed in [Van10, Wanders11]). In plant cells, on the other hand, the major sites are the peroxisome and glyoxysome (a specialized peroxisome found only in germinating seeds). The mitochondrion is also active, but is most likely responsible only for degradation of branched-chain fatty acids.
Another major difference lies in the structure of the enzymes. In animal mitochondria, after initial metabolism of long chain acyl-CoAs by membrane-bound enzymes, medium and short chain acyl-CoAs are metabolized in the matrix by separate soluble enzymes. In contrast, plant and animal peroxisomes and plant glyoxysomes contain multifunctional proteins (MFPs) that catalyze multiple steps of the pathway. Plant MFPs appear to have S stereospecificity, whereas the fungal counterparts are R stereospecific (see fatty acid β-oxidation (peroxisome, yeast)). Mammals contain two distinct MFPs, one with S and the other with R stereospecificity (reviewed in [Goepfert07, Poirier06, Van10, Houten10]).
The main biochemical difference between the animal mitochondrial and bacterial β-oxidation pathway (see fatty acid β-oxidation I) and the plant and animal peroxisomal counterpart lies in the first step, which converts an acyl-CoA to a trans-2-enoyl-CoA. In bacteria or animal mitochondria, this reaction is catalyzed by acyl-CoA dehydrogenase. The electrons removed by the oxidation pass through the respiratory chain to oxygen, generating water as the final product. In plant and animal peroxisomes, this reaction is catalyzed by acyl-CoA oxidase. The electrons pass directly to oxygen and produce hydrogen peroxide, which is immediately cleaved by peroxisomal catalases.
It is still debated whether fatty acids are activated to acyl-CoAs prior to or after their transport into peroxisomes. Two peroxisomal acyl-CoA synthetases have been recently identified and characterized from Arabidopsis thaliana col [Fulda02]. Both enzymes are able to activate the full spectrum of fatty acids naturally found in the seed, and both genes are strongly induced during seed germination. These observations suggest that the two peroxisomal enzymes are involved in the fatty acid β-oxidation pathway. Reviewed in [Graham02b].
Superpathways: superpathway of glyoxylate cycle and fatty acid degradation
Variants: 9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast) , 10-cis-heptadecenoyl-CoA degradation (yeast) , 10-trans-heptadecenoyl-CoA degradation (MFE-dependent, yeast) , 10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast) , alkane oxidation , fatty acid α-oxidation I , fatty acid α-oxidation II , fatty acid α-oxidation III , fatty acid β-oxidation (peroxisome, yeast) , fatty acid β-oxidation I , fatty acid β-oxidation III (unsaturated, odd number) , fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent) , fatty acid β-oxidation VI (peroxisome) , oleate β-oxidation , oleate β-oxidation (isomerase-dependent, yeast) , oleate β-oxidation (reductase-dependent, yeast) , oleate β-oxidation (thioesterase-dependent, yeast) , unsaturated, even numbered fatty acid β-oxidation
Adham05: Adham AR, Zolman BK, Millius A, Bartel B (2005). "Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation." Plant J 41(6);859-74. PMID: 15743450
Begrends88: Begrends, Wilke, Engeland, Kurt, Kindl, Helmut (1988). "Characterization of two forms of the multifunctional protein acting in fatty acid beta-oxidation." Arch Biochem Biophys, 263(1): 161-1691.
Fulda02: Fulda M, Shockey J, Werber M, Wolter FP, Heinz E (2002). "Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation." Plant J 32(1);93-103. PMID: 12366803
Germain01: Germain V, Rylott EL, Larson TR, Sherson SM, Bechtold N, Carde JP, Bryce JH, Graham IA, Smith SM (2001). "Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings." Plant J 28(1);1-12. PMID: 11696182
GuhnemannShafer94: Guhnemann-Shafer, Kerstin, Engeland, Kurt, Linder, Dietmar, Kindl, Helmut (1994). "Evidence for domain structures of the trifunctional protein and tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation." Eur J Biochem, 226: 909-915.
Campbell03: Campbell JW, Morgan-Kiss RM, E Cronan J (2003). "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Mol Microbiol 47(3);793-805. PMID: 12535077
Cao08: Cao W, Liu N, Tang S, Bao L, Shen L, Yuan H, Zhao X, Lu H (2008). "Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of BNIP3 in two human cell lines." Biochim Biophys Acta 1780(6);873-80. PMID: 18371312
Dmochowska90: Dmochowska A, Dignard D, Maleszka R, Thomas DY (1990). "Structure and transcriptional control of the Saccharomyces cerevisiae POX1 gene encoding acyl-coenzyme A oxidase." Gene 88(2);247-52. PMID: 2189786
Einerhand91: Einerhand AW, Voorn-Brouwer TM, Erdmann R, Kunau WH, Tabak HF (1991). "Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae." Eur J Biochem 200(1);113-22. PMID: 1715273
Ferdinandusse00: Ferdinandusse S, Denis S, van Berkel E, Dacremont G, Wanders RJ (2000). "Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method." J Lipid Res 41(3);336-42. PMID: 10706581
Ferdinandusse04: Ferdinandusse S, Denis S, Van Roermund CW, Wanders RJ, Dacremont G (2004). "Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids." J Lipid Res 45(6);1104-11. PMID: 15060085
Ferdinandusse07: Ferdinandusse S, Denis S, Hogenhout EM, Koster J, van Roermund CW, IJlst L, Moser AB, Wanders RJ, Waterham HR (2007). "Clinical, biochemical, and mutational spectrum of peroxisomal acyl-coenzyme A oxidase deficiency." Hum Mutat 28(9);904-12. PMID: 17458872
GuhnemannSchafe95: Guhnemann-Schafer K, Kindl H (1995). "Fatty acid beta-oxidation in glyoxysomes. Characterization of a new tetrafunctional protein (MFP III)." Biochim Biophys Acta 1256(2);181-6. PMID: 7766696
Gurvitz01: Gurvitz A, Hiltunen JK, Erdmann R, Hamilton B, Hartig A, Ruis H, Rottensteiner H (2001). "Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11." J Biol Chem 276(34);31825-30. PMID: 11431484
Harwood94: Harwood CS, Nichols NN, Kim MK, Ditty JL, Parales RE (1994). "Identification of the pcaRKF gene cluster from Pseudomonas putida: involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate." J Bacteriol 176(21);6479-88. PMID: 7961399
Hettema96: Hettema EH, van Roermund CW, Distel B, van den Berg M, Vilela C, Rodrigues-Pousada C, Wanders RJ, Tabak HF (1996). "The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae." EMBO J 15(15);3813-22. PMID: 8670886
Johnson94: Johnson DR, Knoll LJ, Levin DE, Gordon JI (1994). "Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism." J Cell Biol 127(3);751-62. PMID: 7962057
Johnson94a: Johnson DR, Knoll LJ, Rowley N, Gordon JI (1994). "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA synthetase genes in regulating protein N-myristoylation." J Biol Chem 269(27);18037-46. PMID: 8027063
Kameda85a: Kameda K, Suzuki LK, Imai Y (1985). "Further purification, characterization and salt activation of acyl-CoA synthetase from Escherichia coli." Biochim Biophys Acta 1985;840(1);29-36. PMID: 3888279
Katsuyama10: Katsuyama Y, Ohnishi Y, Horinouchi S (2010). "Production of dehydrogingerdione derivatives in Escherichia coli by exploiting a curcuminoid synthase from Oryza sativa and a β-oxidation pathway from Saccharomyces cerevisiae." Chembiochem 11(14);2034-41. PMID: 20836122
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