The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties.

摘要: cDNA clones corresponding to two alleles of the ADH3 locus were identified by hybridization with synthetic oligodeoxyribonucleotides specific for class I human liver alcohol dehydrogenase. Sequences determined a 1457-nucleotide cDNA, covering whole γ2-coding region, and 1224-nucleotide including region coding amino acid residues 53–374 γ1 subunit. Two replacements between γ2 subunits identified. At position 349, isoleucine in instead valine is conservative exchange superficial residue which has been ascribed no special importance. The other exchange, at 271, arginine glutamine γ2, explains differences enzyme properties. Electrophoretically, it consistent less cathodic mobility Functionally, location surface coenzyme-binding pocket may influence dissociation reduced coenzyme.