Structural relationships among aldehyde dehydrogenases
| Autor: | Hans Jörnvall, Jihn Hempel, Hedvig von Bahr-Lindström |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Pharmacology
Cytoplasm Clinical Biochemistry Aldehyde dehydrogenase Mitochondria Liver Aldehyde Dehydrogenase Biology Toxicology Aldehyde Oxidoreductases Biochemistry Isozyme Peptide Fragments Isoenzymes Structure-Activity Relationship Behavioral Neuroscience Liver biology.protein Animals Humans Amino Acid Sequence Horses Biological Psychiatry |
| Zdroj: | Pharmacology Biochemistry and Behavior. 18:117-121 |
| ISSN: | 0091-3057 |
| DOI: | 10.1016/0091-3057(83)90157-0 |
| Popis: | Two functional regions of liver aldehyde dehydrogenase were characterized before; other structures of homologous parts from isoenzymes have now been determined to obtain further information on the isoenzyme relationships. In a 22-residue region from the horse cytoplasmic and mitochondrial isoenzymes, substitutions occur at 12 positions, including a continuous six-residue portion characterized by non-conservative changes. In contrast, the same structure from the cytoplasmic isoenzyme shows exchanges at only three positions when compared to its counterpart from human cytoplasm. A similar estimate of substitution frequency between species is obtained from a larger sampling at 236 positions. Thus, the isoenzyme difference between aldehyde dehydrogenase from the same species is about five-fold greater than the species difference between corresponding isoenzymes. Hence, the relationship between cytoplasmic and mitochondrial aldehyde dehydrogenases, while recognizable, is distant. This is compatible with the fact that a property such as high sensitivity to disulfiram is a characteristic of only the cytoplasmic isoenzyme. |
| Databáze: | OpenAIRE |
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