Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria.

@article{FaivreNitschke2001PurificationCA,
  title={Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria.},
  author={S E Faivre-Nitschke and Ivan Cou{\'e}e and Matthieu Vermel and J. M. Grienenberger and Jos{\'e} M. Gualberto},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 5},
  pages={1332-9}
}
Between the different types of Acyl-CoA dehydrogenases (ACADs), those specific for branched chain acyl-CoA derivatives are involved in the catabolism of amino acids. In mammals, isovaleryl-CoA dehydrogenase (IVD), an enzyme of the leucine catabolic pathway, is a mitochondrial protein, as other acyl-CoA dehydrogenases involved in fatty acid beta-oxidation. In plants, fatty acid beta-oxidation takes place mainly in peroxisomes, and the cellular location of the enzymes involved in the catabolism… CONTINUE READING

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