AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A. nidulans. 2010

Kathrin Reiser, and Meryl A Davis, and Michael J Hynes
Department of Genetics, University of Melbourne, Parkville, VIC 3010, Australia.

Filamentous fungi can use a variety of fatty acids (FA) as sole carbon and energy sources. Aspergillus nidulans has been shown to possess both peroxisomal and mitochondrial beta-oxidation pathways. In these studies, the major peroxisomal long chain fatty acyl coenzyme A oxidase AoxA was identified. AoxA was shown to be localised to peroxisomes and deletion of the aoxA gene leads to reduced growth on long chain FA, but not on short chain FA. AoxA is predicted to be part of the same peroxisomal beta-oxidation pathway as the bifunctional protein FoxA. In addition, an aoxA(p)lacZ reporter gene construct is induced by short and long chain FA and the induction is dependent on the transcriptional regulators FarA, FarB and ScfA with FarA being required for the induction by short chain as well as long chain FA and FarB and ScfA being required for induction of aoxA by short chain FA. It is proposed that there are additional peroxisomal beta-oxidation pathways in A. nidulans, which include fatty acyl-CoA dehydrogenases with a partially overlapping substrate range and include a pathway for short chain FA.

UI MeSH Term Description Entries
D008928 Mitochondria Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed) Mitochondrial Contraction,Mitochondrion,Contraction, Mitochondrial,Contractions, Mitochondrial,Mitochondrial Contractions
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D005227 Fatty Acids Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed) Aliphatic Acid,Esterified Fatty Acid,Fatty Acid,Fatty Acids, Esterified,Fatty Acids, Saturated,Saturated Fatty Acid,Aliphatic Acids,Acid, Aliphatic,Acid, Esterified Fatty,Acid, Saturated Fatty,Esterified Fatty Acids,Fatty Acid, Esterified,Fatty Acid, Saturated,Saturated Fatty Acids
D001233 Aspergillus nidulans A species of imperfect fungi from which the antibiotic nidulin is obtained. Its teleomorph is Emericella nidulans. Aspergillus nidulellus,Emericella nidulans
D042962 Acyl-CoA Oxidase An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor. Acyl Coenzyme A Oxidase,Fatty Acid Acyl-CoA Oxidase,Fatty Acyl-CoA Oxidase,Fatty Acyl-Coenzyme A Oxidase,Acyl CoA Oxidase,Acyl-CoA Oxidase, Fatty,Fatty Acid Acyl CoA Oxidase,Fatty Acyl CoA Oxidase,Fatty Acyl Coenzyme A Oxidase,Oxidase, Acyl-CoA,Oxidase, Fatty Acyl-CoA
D042964 Acyl-CoA Dehydrogenase A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE. Acyl-coenzyme A Dehydrogenase,Fatty-acyl CoA Dehydrogenase,MCACA-Dehydrogenase,Medium Chain Acyl-CoA Dehydrogenase,Medium-Chain Acyl-CoA Dehydrogenase,Medium-Chain Acyl-Coenzyme A Dehydrogenase,Octanoyl-CoA Dehydrogenase,Palmitoyl-CoA Dehydrogenase,Acyl CoA Dehydrogenase,Acyl coenzyme A Dehydrogenase,Acyl-CoA Dehydrogenase, Medium-Chain,CoA Dehydrogenase, Fatty-acyl,Dehydrogenase, Acyl-CoA,Dehydrogenase, Acyl-coenzyme A,Dehydrogenase, Fatty-acyl CoA,Dehydrogenase, Medium-Chain Acyl-CoA,Dehydrogenase, Octanoyl-CoA,Dehydrogenase, Palmitoyl-CoA,Fatty acyl CoA Dehydrogenase,MCACA Dehydrogenase,Medium Chain Acyl CoA Dehydrogenase,Medium Chain Acyl Coenzyme A Dehydrogenase,Octanoyl CoA Dehydrogenase,Palmitoyl CoA Dehydrogenase
D044944 Acyl-CoA Dehydrogenases Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS. Acyl CoA Dehydrogenases,Dehydrogenases, Acyl-CoA
D017930 Genes, Reporter Genes whose expression is easily detectable and therefore used to study promoter activity at many positions in a target genome. In recombinant DNA technology, these genes may be attached to a promoter region of interest. Reporter Genes,Gene, Reporter,Reporter Gene
D020675 Peroxisomes Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed) Peroxisome

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