Substitutions of a buried glutamate residue hinder the conformational change in horse liver alcohol dehydrogenase and yield a surprising complex with endogenous 3â²-Dephosphocoenzyme A
Keywords: اتصال کوآنزیم; Enzyme kinetics; Coenzyme binding; Conformational change; Hydride transfer; X-ray crystallography; Protein structure; ADH; alcohol dehydrogenase; E267H; substitution Glu-267 with histidine residue; E267â¯H/N; substitution with either histidine or asparag