Alcohol:NAD+ oxidoreductase is present in rat liver peroxisomes.
Alcohol:NAD+ oxidoreductase was found in the peroxisomes of animal liver for the first time as follows. The distribution of alcohol:NAD+ oxidoreductase activity with nonanol as substrate in the light mitochondrial fraction (peroxisome-enriched fraction) of rat liver was examined by centrifugation in a sucrose density gradient. Most of the enzyme activity was localized in the mitochondria, with some activity in the peroxisomes. The administration of clofibrate, a peroxisome proliferator, to rats resulted in a marked increase of the enzyme activity in the peroxisomes, but not in the mitochondria. The enzyme was found to be located in the matrix of the peroxisomes. The evidence was obtained that the enzyme differed from alcohol dehydrogenases and alcohol oxidizing systems found previously. The enzyme activity was not affected by pyrazole, an inhibitor of alcohol dehydrogenase and sodium azide, an inhibitor of catalase. The enzyme was NAD(+)-dependent and oxidized straight chain aliphatic alcohols with a variety of carbon chains (C2-C18), showing the maximum on nonanol. Km values toward these aliphatic alcohols decreased with increasing chain length. The major reaction product was identified as the carboxylic acid by using high performance liquid chromatography.
Sakuraba
H
H
Department of Biochemistry, Kyushu Dental College, Kitakyushu, Japan.
Noguchi
T
T
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000818:Animals; D002994:Clofibrate / Q000494:pharmacology; D007700:Kinetics; D008830:Microbodies / Q000187:drug effects / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D051381:Rats
D000426:Alcohol Dehydrogenase; D002994:Clofibrate