Mitochondrial alcohol dehydrogenase from ethanol-grown Euglena gracilis.
The inducing effects of ethanol on alcohol dehydrogenase and the key enzymes of the glyoxylate cycle, isocitrate lyase and malate synthase, in Euglena cells were investigated. Ethanol as the sole carbon source resulted in increases in alcohol dehydrogenase and the two glyoxylate cycle enzymes. The experimental results indicated that ethanol is assimilated by alcohol dehydrogenase and the glyoxylate cycle in Euglena. Mitochondria from aerobically grown Euglena contain a unique type of alcohol dehydrogenase that accounts for their ability to respire with ethanol as a substrate. This alcohol dehydrogenase was purified to homogeneity from ethanol-grown Euglena gracilis. The mitochondrial alcohol dehydrogenase was NAD(+)-specific but not NADP(+)-specific. Ethanol was the most active substrate, but the enzyme was also active towards 1-butanol, 1-heptanol, cinnamyl alcohol, and myristyl alcohol. These results indicated that mitochondrial alcohol dehydrogenase participated in alcohol metabolism in Euglena gracilis.
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D000438:Alcohols / Q000378:metabolism; D000818:Animals; D002458:Cell Fractionation; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D000431:Ethanol / Q000378:metabolism*; D005056:Euglena gracilis / Q000201:enzymology*; D015971:Gene Expression Regulation, Enzymologic; D005936:Glucans / Q000378:metabolism; D007522:Isocitrate Lyase / Q000378:metabolism; D008292:Malate Synthase / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010101:Oxygen Consumption; D011134:Polysaccharides / Q000096:biosynthesis; D013379:Substrate Specificity
D000438:Alcohols; D003470:Culture Media; D005936:Glucans; D011134:Polysaccharides; D009243:NAD; D000431:Ethanol; C003045:paramylon; D000426:Alcohol Dehydrogenase; D008292:Malate Synthase; D007522:Isocitrate Lyase