Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus

Biochem J. 1986 Nov 1;239(3):517-22. doi: 10.1042/bj2390517.


Glucose dehydrogenase has been purified to homogeneity from cell extracts of the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus. The enzyme utilizes both NAD+ and NADP+ as coenzyme and catalyses the oxidation of several monosaccharides to the corresponding glyconic acid. Substrate specificity and oxidation rate depend on the coenzyme present; when NAD+ is used, the enzyme binds and oxidizes specifically sugars presenting equatorial orientation of hydroxy groups at C-2, C-3 and C-4. The Mr of the native enzyme is 124,000 and decreases to about 60,000 in the presence of 6 M-guanidinium chloride and to about 30,000 in the presence of 5% (w/v) SDS. The enzyme shows maximal activity at pH 9, 77 degrees C and 20 mM-Mg2+, -Mn2+ or -Ca2+ and is fairly stable in the presence of chaotropic agents and water-miscible organic solvents such as methanol or acetone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Carbohydrate Conformation
  • Carbohydrate Dehydrogenases / metabolism*
  • Galactose / metabolism
  • Glucose / metabolism
  • Glucose 1-Dehydrogenase
  • Glucose Dehydrogenases / isolation & purification
  • Glucose Dehydrogenases / metabolism*
  • Kinetics
  • Molecular Weight
  • Substrate Specificity
  • Thermoplasma / enzymology*
  • Xylose / metabolism


  • Amino Acids
  • Xylose
  • Carbohydrate Dehydrogenases
  • Glucose Dehydrogenases
  • Glucose 1-Dehydrogenase
  • Glucose
  • Galactose