Mutation of serine-39 to threonine in thermostable secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus changes enantiospecificity

Research was conducted to investigate the impact of the mutation of Ser39 to threonine on the enantiospecificity and regiospecificity of secondary alcohol dehydrogenases (SADH) from Thermoanaerobacter ethanolicus. This is the first experiment demonstrating a single mutation that results in significant effects on the enantiospecificity of an enzyme. Results indicate that (S)-2 butanol specificity decreased while (R)-2-pentanol specificity was enhanced due to mutation.