[Interaction of ethanolamine with alcohol dehydrogenase from the horse liver].
The pattern of kinetic behaviour of ethanolamine (EA), an ethanol structural analog, in the alcohol dehydrogenase reaction has been studied. EA has been shown to manifest a mixed type inhibition versus ethanol and a noncompetitive behaviour towards the second substrate, NAD. A graphical analysis of the experimental results as well as the construction of secondary graphs provide evidence in favour of a mechanism, according to which the interaction between EA and the enzyme results in a dead-end complex formation (ESI). A direct conversion into reaction products can be achieved only after EA separation from the complex. The Ki value for the E-EA complex is 1.3 mM; that for EA release from the E-EA is 1.8 mM. An analysis of competitive interactions with NAD showed these constants to be equal in values (2 mM). Taking account of real concentrations of tissue EA and of experimental values of Ki, a conclusion is drawn on possible participation of EA in the alcohol dehydrogenase reaction control.
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D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D000431:Ethanol / Q000378:metabolism / Q000494:pharmacology; D019856:Ethanolamine; D004983:Ethanolamines / Q000378:metabolism / Q000494:pharmacology*; D006736:Horses; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D013379:Substrate Specificity
D004983:Ethanolamines; D000431:Ethanol; D019856:Ethanolamine; D000426:Alcohol Dehydrogenase
Izuchenie vzaimodeĭstviia étanolamina s alkogol'degidrogenazoĭ iz pecheni loshadi.