Multifunctionality of liver alcohol dehydrogenase. Studies of aldehyde dehydrogenase activity |
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Authors: | CS Tsai DS Sher |
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Institution: | Department of Chemistry and Institute of Biochemistry, Carleton University, Ottawa, Ontario, K1S 5B6 Canada |
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Abstract: | Kinetic studies of the liver alcohol dehydrogenase catalyzed dehydrogenation of aldehydes were carried out over a wide range of octanal concentrations. The effect of specific inhibitors of liver alcohol dehydrogenase on aldehyde dehydrogenase activity was examined. The results were consistent with a steady-state random mechanism with the formation of the ternary E · NADH octanal complex at low temperatures. This ternary complex becomes inconspicuous at high temperatures. The aldehyde dehydrogenase activity was found to associate with all ethanol-active isozymes. The dual dehydrogenase reactions are catalyzed by the same molecule, presumably in the region of the same domain. However, the two activities respond differently to structural changes. |
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