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Structural relationships among aldehyde dehydrogenases.

J Hempel, H Von Bahr-Lindström, H Jörnvall

    Pharmacology, Biochemistry, and Behavior
    |January 1, 1983
    PubMed
    Summary
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    Aldehyde dehydrogenase isoenzymes within the same species show greater differences than between species. Cytoplasmic and mitochondrial aldehyde dehydrogenases have a distant evolutionary relationship.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Previous studies characterized functional regions of liver aldehyde dehydrogenase.
    • Understanding isoenzyme relationships requires analyzing homologous structures.

    Purpose of the Study:

    • To determine structures of homologous parts from aldehyde dehydrogenase isoenzymes.
    • To gain further insights into isoenzyme relationships.

    Main Methods:

    • Comparative sequence analysis of specific residue regions (22-residue and 236-position) between horse cytoplasmic and mitochondrial isoenzymes.
    • Comparison of human and horse cytoplasmic isoenzymes.
    • Analysis of substitution frequencies.

    Main Results:

    Related Experiment Videos

  • A 22-residue region showed 12 substitutions between horse cytoplasmic and mitochondrial isoenzymes, including non-conservative changes.
  • Comparing human and horse cytoplasmic isoenzymes revealed only three substitutions in the same region.
  • A larger 236-position analysis indicated a five-fold greater difference between isoenzymes of the same species compared to species differences between corresponding isoenzymes.

    • Conclusions:

    • The evolutionary relationship between cytoplasmic and mitochondrial aldehyde dehydrogenases is distant, despite being recognizable.
    • This distant relationship is supported by functional differences, such as high sensitivity to disulfiram in the cytoplasmic isoenzyme only.