Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system

His-48 in yeast alcohol dehydrogenase I (His 51 in horse liver alcohol dehydrogenase) is a highly conserved residue in the active sites of many alcohol dehydrogenases. The imidazole group of His-48 may participate in base catalysis of proton transfer as it is linked by hydrogen bonds through the 2′-...

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Veröffentlicht in:	Chemico-biological interactions 2023-09, Vol.382, p.110558-110558, Article 110558
Hauptverfasser:	Plapp, Bryce V., Kratzer, Darla Ann, Souhrada, Susan K., Warth, Edda, Jacobi, Tobias
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetaldehyde Alcohol Dehydrogenase - metabolism Animals Catalysis Deuterium Enzyme kinetics Enzyme mechanism Ethanol Glutamic Acid Histidine Horses Hydrogen-Ion Concentration Hydroxide catalysis Kinetics Mutagenesis Mutagenesis, Site-Directed NAD - metabolism Proton transfer Protons Saccharomyces cerevisiae - metabolism Serine
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