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A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a ‘High‐ K m ,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism
Author(s) -
Algar Elizabeth M.,
VandeBerg John L.,
Holmes Roger S.
Publication year - 1992
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.1530-0277.1992.tb01894.x
Subject(s) - baboon , alcohol dehydrogenase , alcohol , aldehyde dehydrogenase , ethanol , enzyme , ethanol metabolism , isozyme , metabolism , alcohol oxidoreductase , chemistry , substrate (aquarium) , biochemistry , alcohol tolerance , biology , endocrinology , nad+ kinase , ecology
The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using K cat / K m , values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed ‘high‐ K m ’ properties with respect to ethanol, and is expected to significantly contribute to ‘first‐pass’ metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver ‘low‐ K m ’ ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.