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Human Aldehyde Dehydrogenase: Metabolism of Putrescine and Histamine
Author(s) -
Ambroziak Wojciech,
Pietruszko Regina
Publication year - 1987
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1987.tb00167.x
Subject(s) - putrescine , histamine , aldehyde dehydrogenase , metabolism , biochemistry , chemistry , biology , enzyme , pharmacology
Imidazoleacetaldehyde and γ‐aminobutyraldehyde, metabolites of histamine and putrescine, respectively, have been shown to be substrates of human liver aldehyde dehydrogenase (EC 1.2.1.3) cytoplasmic (E1) and mitochondrial (E2) isozymes. The K m values at pH 7.4 and 500 μM NAD for imidazoleacetaldehyde and γ‐aminobutyraldehyde for the E1 isozyme are 40 and 800 μM, respectively, and for the E2 isozyme are 50 and 500 μM, respectively. The K m values with γ‐aminobutyraldehyde with both isozymes are high relative to K m values with acetaldehyde (50 μM for E1 and 1 μM for E2). Since activity with both imidazoleacetaldehyde and γ‐aminobutyraldehyde in crude liver homogenates paralleled that of aldehyde dehydrogenase (EC 1.2.1.3) during purification it appears likely that in the human liver this enzyme is responsible for metabolism of both compounds. If this is the case, interaction between metabolism of histamine and putrescine and that of alcohol is likely. Both imidazoleacetaldehyde and γ‐aminobutyraldehyde were synthesized in this laboratory and their stability has been investigated. Procedures for assaying aldehyde dehydrogenase employing synthetic metabolites of histamine and putrescine are provided.