Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species

The kinetic and thermodynamic properties of the Sulfolobus sp. strain RC3 and Sulfolobus solfataricus alcohol dehydrogenase were examined by overexpressing each species' adh gene in Escherichia coli. Results revealed that only 17 amino acid replacements caused differences in the two enzymes' thermal activities and substrate specificities. Amino-terminal residues were found to have a substantial effect on the efficiency and specificity of alcohol-dehydrogenases.