NAD(-DEHYDROGENASE FOR SULFOLOBUS-SOLFATARICUS - STRUCTURAL AND FUNCTIONAL FEATURES() DEPENDENT ALCOHOL)

Alcohol dehydrogenase, EC 1.1.1.1 (ADH), from the thermophilic archaeb acterium Sulfolobus solfataricus (SsADH) is a strictly NAD(+)-dependen t enzyme with an amino acid sequence related to those of horse liver, yeast and Thermoanaerobium brockii ADHs. This enzyme is remarkably the rmophilic and thermostable; protein stability is strictly dependent on the presence of structural zinc in the molecule. For its broad substr ate specificity, product stereoselectivity and acceptance of NAD(+)-ma cromolecular derivatives, SsADH appears suitable for laboratory-scale chemoselective synthesis. Moreover, it represents a useful protein mod el for studying the structure-function-stability relationships in ther mophilic enzymes.