Subcellular localization of aldehyde reductase activities in ox brain.
The distribution of the two principal isoenzymes of aldehyde reductase (EC 1.1.1.2) has been studied in ox brain. The more active of these, which has been termed the high-Km enzyme, has been shown to be located in the cytosol and the less abundant low-Km form has a similar localization. p-Nitrobenzaldehyde, which has been used as a substrate in previous studies, caused the reduction of NADH in the presence of the mitochondrial fraction, but mixed substrate experiments with 1,3-dinitrobenzene and the effects of pH on the activity indicate that this is due to the presence of a nitro reductase activity which has been recently described (Köchli, Wermuth & von Wartburg (1980) Biochim. Biophys. Acta 616, 133-142] rather than to the low-Km aldehyde reductase activity. Fractionation of the mitochondria indicated this activity to be largely confined to the mitochondrial inner membrane.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002458:Cell Fractionation; D004072:Digitonin / Q000494:pharmacology; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D011725:Pyridines / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology; D013367:Submitochondrial Particles / Q000201:enzymology
D000447:Aldehydes; D001547:Benzaldehydes; D007527:Isoenzymes; D011725:Pyridines; C033525:4-carboxybenzaladehyde; C014785:3-pyridinaldehyde; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+); D005969:Glutamate Dehydrogenase; D004072:Digitonin