Catalytic and FAD-binding Residues of Mitochondrial Very Long Chain Acyl-Coenzyme A Dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase.
2. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients.
3. Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein.
4. Evidence for Intermediate Channeling in Mitochondrial β -Oxidation
5. Purification and Properties of Rat Liver Acyl-CoA Dehydrogenases and Electron Transfer Flavoprotein1
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1. Weak electric field strengthens the β-oxidation degradation of fatty acids by activated sludge to produce micro-nano CaCO3;Journal of Environmental Chemical Engineering;2024-08
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3. Fatty Acid Oxidation Is Required for Myxococcus xanthus Development;Journal of Bacteriology;2018-05-15
4. Identification of the Catalytic Residue of Rat Acyl-CoA Dehydrogenase 9 by Site-Directed Mutagenesis;Applied Biochemistry and Biotechnology;2017-01-13
5. ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies;Human Molecular Genetics;2013-10-24
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