Cephalopod alcohol dehydrogenase: purification and enzymatic characterization.
Octopus, squid and cuttle-fish organs were examined for alcohol dehydrogenase activity. Only one form was detectable, with properties typical of mammalian class III alcohol dehydrogenase. The corresponding protein was purified from octopus and enzymatically characterized. Ion-exchange and affinity chromatography produced a pure protein in excellent yield (73%) after 1600-fold purification. Enzymatic parameters with several substrates were similar to those for the human class III alcohol dehydrogenase, demonstrating a largely conserved function of the enzyme through wide lines of divergence covering vertebrates, cephalopods and bacteria. The results establish the universal occurrence of class III alcohol dehydrogenase and its strictly conserved functional properties in separate living forms. The absence of other alcohol dehydrogenases in cephalopods is compatible with the emergence of the ethanol-active class I type at a later stage, in lineages leading to vertebrates.
Rosario Fernández
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M
Department of Biochemistry and Molecular Biology, Faculty of Sciences, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Jörnvall
H
H
Moreno
A
A
Kaiser
R
R
Parés
X
X
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D049832:Decapodiformes / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004592:Electrophoresis, Starch Gel; D006801:Humans; D008974:Mollusca / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D049831:Octopodiformes / Q000201:enzymology; D013045:Species Specificity; D013379:Substrate Specificity
D009243:NAD; D009249:NADP; D000426:Alcohol Dehydrogenase