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 ω-oxidation
|Superclasses:||Degradation/Utilization/Assimilation → Fatty Acid and Lipids Degradation → Fatty Acids Degradation|
Industrially important yeasts such as Candida cloacae and Candida tropicalis are capable of taking up and utilizing alkanes and long chain fatty acids as sole carbon sources for growth. Alkanes and long chain fatty acids are first metabolized through ω-oxidation. The methyl group at the end of the molecule (the ω carbon) is oxidized to a hydroxyl group, then to an oxo group, and finally to a carboxyl group. The long chain dicarboxylates derived from ω-oxidation then enter the β-oxidation pathway for further degradation.
In alkane-utilizing yeasts the CYP52 subfamily of cytochrome P450s and their corresponding NADPH cytochrome P450 reductases form the monooxygenase system that catalyzes the ω-oxidation steps in the utilization of alkanes and fatty acids [Craft03]. In Candida cloacae and Candida tropicalis the oxidation of the ω-hydroxy group of the intermediate ω-alcohol, or ω-hydroxy fatty acid is catalyzed by an alcohol oxidase [Cheng05a]. This differs from what is known of ω oxidation in other species including animals and certain alkane-, or fatty acid-, utilizing bacteria. In those organisms, the conversion is catalyzed by an alcohol dehydrogenase.
The finding of the potential Arabidopsis homolog of the yeast alcohol oxidase suggests that plants may also operate such an ω oxidation pathway. Confirmation of the hypothesis awaits the functional characterization of the homolog and the identification of other enzymes involved in the pathway. The role of the pathway in plants is probably in wax biosynthesis, rather than in fatty acid degradation [Vanhanen00].
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) , 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 II (peroxisome) , 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
Unification Links: AraCyc:PWY-2724
Cheng05a: Cheng Q, Sanglard D, Vanhanen S, Liu HT, Bombelli P, Smith A, Slabas AR (2005). "Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism." Biochim Biophys Acta 1735(3);192-203. PMID: 16046182
Craft03: Craft DL, Madduri KM, Eshoo M, Wilson CR (2003). "Identification and characterization of the CYP52 family of Candida tropicalis ATCC 20336, important for the conversion of fatty acids and alkanes to alpha,omega-dicarboxylic acids." Appl Environ Microbiol 69(10);5983-91. PMID: 14532053
Smit05: Smit MS, Mokgoro MM, Setati E, Nicaud JM (2005). "alpha,omega-Dicarboxylic acid accumulation by acyl-CoA oxidase deficient mutants of Yarrowia lipolytica." Biotechnol Lett 27(12);859-64. PMID: 16086248
Vanhanen00: Vanhanen S, West M, Kroon JT, Lindner N, Casey J, Cheng Q, Elborough KM, Slabas AR (2000). "A consensus sequence for long-chain fatty-acid alcohol oxidases from Candida identifies a family of genes involved in lipid omega-oxidation in yeast with homologues in plants and bacteria." J Biol Chem 275(6);4445-52. PMID: 10660617
Cheng04a: Cheng Q, Liu HT, Bombelli P, Smith A, Slabas AR (2004). "Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana." FEBS Lett 574(1-3);62-8. PMID: 15358540
Gatter14: Gatter M, Forster A, Bar K, Winter M, Otto C, Petzsch P, Ježková M, Bahr K, Pfeiffer M, Matthaus F, Barth G (2014). "A newly identified fatty alcohol oxidase gene is mainly responsible for the oxidation of long-chain ω-hydroxy fatty acids in Yarrowia lipolytica." FEMS Yeast Res. PMID: 24931727
Iida00: Iida T, Sumita T, Ohta A, Takagi M (2000). "The cytochrome P450ALK multigene family of an n-alkane-assimilating yeast, Yarrowia lipolytica: cloning and characterization of genes coding for new CYP52 family members." Yeast 16(12);1077-87. PMID: 10953079
Kargel96: Kargel E, Menzel R, Honeck H, Vogel F, Bohmer A, Schunck WH (1996). "Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum." Yeast 12(4);333-48. PMID: 8701606
Ohkuma91: Ohkuma M, Hikiji T, Tanimoto T, Schunck WH, Muller HG, Yano K, Takagi M (1991). "Evidence that more than one gene encodes n-alkane-inducible cytochrome P-450s in Candida maltosa, found by two-step gene disruption." Agric Biol Chem 55(7);1757-64. PMID: 1368716
Ohkuma95: Ohkuma M, Masuda Y, Park SM, Ohtomo R, Ohta A, Takagi M (1995). "Evidence that the expression of the gene for NADPH-cytochrome P-450 reductase is n-alkane-inducible in Candida maltosa." Biosci Biotechnol Biochem 59(7);1328-30. PMID: 7545482
Ohkuma98: Ohkuma M, Zimmer T, Iida T, Schunck WH, Ohta A, Takagi M (1998). "Isozyme function of n-alkane-inducible cytochromes P450 in Candida maltosa revealed by sequential gene disruption." J Biol Chem 273(7);3948-53. PMID: 9461581
Saffert00: Saffert A, Hartmann-Schreier J, Schon A, Schreier P (2000). "A dual function alpha-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing alpha-oxidation of fatty acids in plants." Plant Physiol 123(4);1545-52. PMID: 10938370
Scheller94: Scheller U, Kraft R, Schroder KL, Schunck WH (1994). "Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3." J Biol Chem 269(17);12779-83. PMID: 8175690
Scheller96: Scheller U, Zimmer T, Kargel E, Schunck WH (1996). "Characterization of the n-alkane and fatty acid hydroxylating cytochrome P450 forms 52A3 and 52A4." Arch Biochem Biophys 328(2);245-54. PMID: 8645001
Scheller98: Scheller U, Zimmer T, Becher D, Schauer F, Schunck WH (1998). "Oxygenation cascade in conversion of n-alkanes to alpha,omega-dioic acids catalyzed by cytochrome P450 52A3." J Biol Chem 273(49);32528-34. PMID: 9829987
Schunck89: Schunck WH, Kargel E, Gross B, Wiedmann B, Mauersberger S, Kopke K, Kiessling U, Strauss M, Gaestel M, Muller HG (1989). "Molecular cloning and characterization of the primary structure of the alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa." Biochem Biophys Res Commun 161(2);843-50. PMID: 2735924
Schunck91: Schunck WH, Vogel F, Gross B, Kargel E, Mauersberger S, Kopke K, Gengnagel C, Muller HG (1991). "Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum." Eur J Cell Biol 55(2);336-45. PMID: 1935996
Takagi89: Takagi M., Ohkuma M., Kobayashi N., Watanabe M., Yano K. (1989). "Purification of cytochrome P-450alk from n-alkane-grown cells of Candida maltosa, and cloning and nucleotide sequencing of the encoding gene." Agric. Biol. Chem. 53:2217-2226.
Vogel92: Vogel F, Gengnagel C, Kargel E, Muller HG, Schunck WH (1992). "Immunocytochemical localization of alkane-inducible cytochrome P-450 and its NADPH-dependent reductase in the yeast Candida maltosa." Eur J Cell Biol 57(2);285-91. PMID: 1511703
Zimmer96: Zimmer T, Ohkuma M, Ohta A, Takagi M, Schunck WH (1996). "The CYP52 multigene family of Candida maltosa encodes functionally diverse n-alkane-inducible cytochromes P450." Biochem Biophys Res Commun 224(3);784-9. PMID: 8713123
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