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Enzymology and Molecular Biology of Carbonyl Metabolism 5

Volume 372 of the series Advances in Experimental Medicine and Biology pp 159-168

Cloning and Characterization of Genes Encoding Four Additional Human Aldehyde Dehydrogenase Isozymes

  • Lily C. HsuAffiliated withDepartment of Biochemical Genetics, Beckman Research Institute of the City of Hope
  • , Wen-Chung ChangAffiliated withDepartment of Biochemical Genetics, Beckman Research Institute of the City of Hope
  • , Sharon W. LinAffiliated withDepartment of Biochemical Genetics, Beckman Research Institute of the City of Hope
  • , Akira YoshidaAffiliated withDepartment of Biochemical Genetics, Beckman Research Institute of the City of Hope

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Abstract

Aldehyde dehydrogenases (ALDH; aldehyde:NAD+ oxidoreductase, EC 1.2.1.3) are a group of isozymes with broad substrate specificity. They catalyze the oxidation of various aliphatic and aromatic aldehydes to the corresponding acids (Pietruszko, 1983) and have been frequently considered as detoxifying enzymes which eliminate aldehydes in vivo. Metabolism of ethanol-derived acetaldehyde and toxic aldehyde in the foodstuff and from lipid peroxidation are examples of the detoxification role of the ALDH isozymes (Parrilla et al, 1974; Harrington et al, 1987; Mitchell et al., 1987; Jakoby et al., 1990). Recently, it has been demonstrated that the enzymes also play crucial roles in the metabolism of retinoic acid, biogenic amine and neurotransmitters (Ambroziak and Pietruszko, 1991, 1993; Yoshida et al., 1992, 1993).