Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis

Primary and secondary kD/kT and kH/kT kinetic isotope effects have been studied as a probe of hydrogen tunneling in the oxidation of benzyl alcohol catalyzed by horse liver alcohol dehydrogenase (LADH). In the case of the wild-type enzyme, isotope effects at 25 degrees C do not clearly support hydro...

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Veröffentlicht in:	Biochemistry (Easton) 1993-06, Vol.32 (21), p.5503-5507
Hauptverfasser:	Bahnson, Brian J, Park, Doo Hong, Kim, Keehyuk, Plapp, Bryce V, Klinman, Judith P
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Horses Kinetics Liver - enzymology Mathematics Models, Molecular Mutagenesis, Site-Directed NAD - metabolism Oxidoreductases Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Thermodynamics
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