Kinetics of A Glycine for Arg-47 Human Alcohol Dehydrogenase Mutant Can be Explained by Lys-228 Recruitment into the Pyrophosphate Binding Site
Chapter
Abstract
Ethanol and other alcohols are metabolized in liver by alcohol dehydrogenase isoenzymes. At least five electrophoretically distinct isoenzymes are found in human liver that can be divided into three classes (Burnell & Bosron, 1989). Class I comprises the a, β, and γ subunits, while class II contains the π subunit and class III contains the χ subunit. In addition, heterogeneity exists at the β and γ loci, producing the β1, β2, and β3 subunits, and the γ1 and γ2 subunits. Although the class II and III subunits associate only with themselves to form active homodimers, the class I isoenzymes associate to form both homodimers and heterodimers. Thus, the liver can contain as many as 17 active alcohol dehydrogenase isoenzyme forms.
Keywords
Alcohol Dehydrogenase Binary Complex Ethanol Oxidation Dissociation Rate Constant Molecular Replacement
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