Characterization of Acyl-CoA Oxidases from the Lipolytic Yeast Candida aaseri SH14
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
The lipolytic yeast Candida aaseri SH14 contains three Acyl-CoA oxidases (ACOXs) which are encoded by the CaAOX2, CaAOX4, and CaAOX5 genes and catalyze the first reaction in the β-oxidation of fatty acids. Here, the respective functions of the three CaAOX isozymes were studied by growth analysis of mutant strains constructed by a combination of three CaAOX mutations in minimal medium containing fatty acid as the sole carbon source. Substrate specificity of the CaAOX isozymes was analyzed using recombinant C. aaseri SH14 strains overexpressing the respective genes. CaAOX2 isozyme showed substrate specificity toward short- and medium-chain fatty acids (C6-C12), while CaAOX5 isozyme preferred long-chain fatty acid longer than C12. CaAOX4 isozyme revealed a preference for a broad substrate spectrum from C6-C16. Although the substrate specificity of CaAOX2 and CaAOX5 covers medium- and long-chain fatty acids, these two isozymes were insufficient for complete β-oxidation of long-chain fatty acids, and therefore CaAOX4 was indispensable.
Abstract
The lipolytic yeast Candida aaseri SH14 contains three Acyl-CoA oxidases (ACOXs) which are encoded by the CaAOX2, CaAOX4, and CaAOX5 genes and catalyze the first reaction in the β-oxidation of fatty acids. Here, the respective functions of the three CaAOX isozymes were studied by growth analysis of mutant strains constructed by a combination of three CaAOX mutations in minimal medium containing fatty acid as the sole carbon source. Substrate specificity of the CaAOX isozymes was analyzed using recombinant C. aaseri SH14 strains overexpressing the respective genes. CaAOX2 isozyme showed substrate specificity toward short- and medium-chain fatty acids (C6-C12), while CaAOX5 isozyme preferred long-chain fatty acid longer than C12. CaAOX4 isozyme revealed a preference for a broad substrate spectrum from C6-C16. Although the substrate specificity of CaAOX2 and CaAOX5 covers medium- and long-chain fatty acids, these two isozymes were insufficient for complete β-oxidation of long-chain fatty acids, and therefore CaAOX4 was indispensable.
참고문헌 (23)
- Lee SH, "Draft genome sequence of a lipolytic yeast, Candida aaseri SH-14", Genome Announc, 5, pp.00373~00317 (2017)
- Hilmi Ibrahim Z, "Genetic manipulation of a lipolytic yeast Candida aaseri SH14 using CRISPR-Cas9 system", Microorganisms, 8, pp.526~ (2020)
- Hunt MC, "Regulation of peroxisomal lipid metabolism : the role of acyl-CoA and coenzyme A metabolizing enzymes", Biochimie, 98, pp.45~55 (2014)
- Poirier Y, "Peroxisomal beta-oxidation--a metabolic pathway with multiple functions", Biochim. Biophys. Acta, 1763, pp.1413~1426 (2006)
- Hashimoto T, "Peroxisomal beta-oxidation enzymes", Neurochem. Res, 24, pp.551~563 (1999)
- Nakajima Y, "Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase", J. Biochem, 131, pp.365~374 (2002)
- Beites T, "Multiple acyl-CoA dehydrogenase deficiency kills Mycobacterium tuberculosis in vitro and during infection", Nat. Commun, 12, pp.6593~ (2021)
- Chen L, "Engineering the Saccharomyces cerevisiae beta-oxidation pathway to increase medium chain fatty acid production as potential biofuel", PLoS One, 9, pp.e84853~ (2014)
- Mlickova K, "Lipid accumulation, lipid body formation, and acyl coenzyme A oxidases of the yeast Yarrowia lipolytica", Appl. Environ. Microbiol, 70, pp.3918~3924 (2004)
- Picataggio S, "Determination of Candida tropicalis acyl coenzyme A oxidase isozyme function by sequential gene disruption", Mol. Cell. Biol, 11, pp.4333~4339 (1991)
- Wang HJ, "Evaluation of acyl coenzyme A oxidase(Aox)isozyme function in the n-alkane-assimilating yeast Yarrowia lipolytica", J. Bacteriol, 181, pp.5140~5148 (1999)
- Warnke M, "Functional characterization of three specific acyl-coenzyme A synthetases involved in anaerobic cholesterol degradation in Sterolibacterium denitrificans Chol1S", Appl. Environ. Microbiol, 84, pp.02721~02717 (2018)
- Arent S, "Structure and function of plant acyl-CoA oxidases", Plant Physiol. Biochem, 46, pp.292~301 (2008)
- De Bellis L, "Purification and characterization of a novel pumpkin short-chain acyl-coenzyme A oxidase with structural similarity to acyl-coenzyme A dehydrogenases", Plant Physiol, 123, pp.327~334 (2000)
- Froman BE, "ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis", Plant Physiol, 123, pp.733~742 (2000)
- Xin Z, "The involvement of a herbivore-induced acyl-CoA oxidase gene, CsACX1, in the synthesis of jasmonic acid and its expression in flower opening in tea plant(Camellia sinensis)", Plant Physiol. Biochem, 135, pp.132~140 (2019)
- Ferdinandusse S, "A novel case of ACOX2 deficiency leads to recognition of a third human peroxisomal acyl-CoA oxidase", Biochim. Biophys. Acta Mol. Basis Dis, 1864, pp.952~958 (2018)
- Morais S, "Conserved expression of alternative splicing variants of peroxisomal acyl-CoA oxidase 1 in vertebrates and developmental and nutritional regulation in fish", Physiol. Genomics, 28, pp.239~252 (2007)
- Mycka G, "Variability of ACOX1 gene polymorphisms across different horse breeds with regard to selection pressure", Animals, 10, pp.2225~ (2020)
- Zeng J, "Specific inhibition of Acyl-CoA oxidase-1 by an acetylenic acid improves hepatic lipid and reactive oxygen species(ROS)metabolism in rats ded a high fat diet", J. Biol. Chem, 292, pp.3800~3809 (2017)
- Reiser K, "AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A", nidulans. Curr. Genet, 56, pp.139~150 (2010)
- Wang H, "Cloning, sequencing, and characterization of five genes coding for acyl-CoA oxidase isozymes in the yeast Yarrowia lipolytica", Cell Biochem. Biophys, 31, pp.165~174 (1999)
- Wang T, "The POX1 gene encoding peroxisomal acyl-CoA oxidase in Saccharomyces cerevisiae is under the control of multiple regulatory elements", J. Biol. Chem, 269, pp.24480~24485 (1994)