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. 1986 Nov 1;239(3):517–522. doi: 10.1042/bj2390517

Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.

P Giardina, M G de Biasi, M de Rosa, A Gambacorta, V Buonocore
PMCID: PMC1147317  PMID: 3827812

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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