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Human Stomach Aldehyde Dehydrogenase, ALDH3

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Enzymology and Molecular Biology of Carbonyl Metabolism 4

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 328))

Abstract

Aldehyde dehydrogenase (ALDH; aldehyde: NAD+ oxidoreductase, EC 1.2.1.3) activities are observed in most tissues with the highest activity in the liver (Deitrich, 1966). In humans, five liver ALDH isozymes have been purified and characterized and one isozyme, ALDH, has been identified by reverse genetics (Hsu and Chang, 1991). Cytosolic ALDH1, mitochondrial ALDH2, and γ-aminobutyraldehyde dehydrogenase, exhibit low Km values (μM range), while cytosolic ALDH3 and mitochondrial ALDH4 have high Km values (mM range) toward acetaldehyde. ALDH3 is active for oxidation of heptaldehyde and benzaldehyde, and ALDH4 is most active for glutamic γ-semialdehyde as substrate (Forte-McRobbie and Pietruszko, 1986).

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Authors and Affiliations

  1. Department of Biochemical Genetics, Beckman Research Institute of the City of Hope, Duarte, CA, 91010, USA

    Lily C. Hsu & Akira Yoshida

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  1. Lily C. Hsu
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  2. Akira Yoshida
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Editors and Affiliations

  1. Purdue University, West Lafayette, Indiana, USA

    Henry Weiner

  2. Indiana University School of Medicine and Veterans Administration Medical Center, Indianapolis, Indiana, USA

    David W. Crabb

  3. Queens University, Kingston, Ontario, Canada

    T. Geoffrey Flynn

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© 1993 Springer Science+Business Media New York

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Hsu, L.C., Yoshida, A. (1993). Human Stomach Aldehyde Dehydrogenase, ALDH3. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_16

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  • DOI: https://doi.org/10.1007/978-1-4615-2904-0_16

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6259-3

  • Online ISBN: 978-1-4615-2904-0

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