A novel archaebacterial NAD+-dependent alcohol dehydrogenase. Purification and properties

Eur J Biochem. 1987 Sep 15;167(3):475-9. doi: 10.1111/j.1432-1033.1987.tb13361.x.


An NAD+-dependent alcohol dehydrogenase (alcohol: NAD+ oxidoreductase, EC was detected in cellular extracts of the extreme thermophilic archaebacterium Sulfolobus solfataricus. The enzyme was purified to homogeneity and shown to be a dimer with a native molecular mass of 71 kDa by sucrose gradient centrifugation and SDS electrophoresis. The enzyme has a broad substrate specificity that includes linear and branched primary alcohols, linear and cyclic secondary alcohols, linear and cyclic ketones and anisaldehyde. The enzyme has an extraordinary thermophilicity and a remarkable thermostability, and appears to have some properties and a structure different from those previously described for thermophilic alcohol dehydrogenases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Dehydrogenase / isolation & purification*
  • Alcohol Dehydrogenase / metabolism
  • Archaea / enzymology*
  • Bacteria / enzymology*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Substrate Specificity


  • Alcohol Dehydrogenase