Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica.
An NADP-linked, alcohol dehydrogenase from Entamoeba histolytica was purified to apparent homogeneity by Blue Sepharose affinity chromatography. Molecular weights of 130,000 and 30,000 were estimated by gel filtration and by sodium dodecyl sulfate polyacrylamide gel electrophoresis, respectively, suggesting that the enzyme is a tetramer. The enzyme exhibited more than 20-fold selectivity for NADP(H) over NAD(H). Although the purified enzyme acts on both primary and secondary alcohols, higher activity was found with secondary alcohols.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D000438:Alcohols / Q000378:metabolism; D000818:Animals; D002846:Chromatography, Affinity; D004748:Entamoeba histolytica / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D000438:Alcohols; D009249:NADP; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+)