Publications

• An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?

  Haferkamp P., Kutschki S., Treichel J., Hemeda H., Sewczyk K., Hoffmann D., Zaparty M., Siebers B.

  Within the SulfoSYS (Sulfolobus Systems Biology) project, the effect of temperature on a metabolic network is investigated at the systems level. Sulfolobus solfataricus utilizes an unusual branched ED (Entner-Doudoroff) pathway for sugar degradation that is promiscuous for glucose and galactose. I ... >> More

  Within the SulfoSYS (Sulfolobus Systems Biology) project, the effect of temperature on a metabolic network is investigated at the systems level. Sulfolobus solfataricus utilizes an unusual branched ED (Entner-Doudoroff) pathway for sugar degradation that is promiscuous for glucose and galactose. In the course of metabolic pathway reconstruction, a glucose dehydrogenase isoenzyme (GDH-2, SSO3204) was identified. GDH-2 exhibits high similarity to the previously characterized GDH-1 (SSO3003, 61% amino acid identity), but possesses different enzymatic properties, particularly regarding substrate specificity and catalytic efficiency. In contrast with GDH-1, which exhibits broad substrate specificity for C5 and C6 sugars, GDH-2 is absolutely specific for glucose. The comparison of kinetic parameters suggests that GDH-2 might represent the major player in glucose catabolism via the branched ED pathway, whereas GDH-1 might have a dominant role in galactose degradation via the same pathway as well as in different sugar-degradation pathways. << Less

  Biochem Soc Trans 39:77-81(2011) [PubMed] [EuropePMC]

• Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.

  Smith L.D., Budgen N., Bungard S.J., Danson M.J., Hough D.W.

  Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/-3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to ... >> More

  Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/-3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to a variety of organic solvents. The amino acid composition was determined and compared with those of the glucose dehydrogenases from the archaebacterium Sulfolobus solfataricus and the eubacteria Bacillus subtilis and Bacillus megaterium. The N-terminal amino acid sequence of the Thermoplasma acidophilum enzyme was determined to be: (S/T)-E-Q-K-A-I-V-T-D-A-P-K-G-G-V-K-Y-T-T-I-D-M-P-E. << Less

  Biochem. J. 261:973-977(1989) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.

  Giardina P., de Biasi M.G., de Rosa M., Gambacorta A., Buonocore V.

  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. Substra ... >> More

  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. << Less

  Biochem. J. 239:517-522(1986) [PubMed] [EuropePMC]

  This publication is cited by 4 other entries.

• Antiviral therapy in AIDS. Clinical pharmacological properties and therapeutic experience to date.

  Sandstrom E.G., Kaplan J.C.

  The rapid spread of human immunodeficiency virus (HIV) infections and the grim outcome of these infections have focused interest on the possibilities for medical intervention. The end-stage of these infections, acquired immune deficiency syndrome (AIDS), was first recognised in 1981, and the causa ... >> More

  The rapid spread of human immunodeficiency virus (HIV) infections and the grim outcome of these infections have focused interest on the possibilities for medical intervention. The end-stage of these infections, acquired immune deficiency syndrome (AIDS), was first recognised in 1981, and the causative agent isolated in 1983. Already several antiviral drugs have been investigated. One initially promising drug, suramin, was found to have a net harmful effect but another, zidovudine (azidothymidine) has been shown to prolong life in AIDS patients. The properties of these and several other antiviral drugs such as antimoniotungstate (HPA-23), foscarnet (phosphonoformate) ribavirin, dideoxynucleotides, and interferons, are reviewed. The role of immunomodulating modalities such as plasmapheresis, bone marrow transplantation, thymosin, interleukin-2, inosine pranobex (isoprinosine), and cyclosporin are also discussed. None of the currently available drugs hold promise as monotherapy. Through analysis of the experience with these drugs and the increasing knowledge of HIV pathogenesis, new drugs can be designed. It seems increasingly clear that drugs will eventually have to be used in combination in order to reduce toxicity, exploit therapeutic synergy, and reduce the risk of HIV resistance. The theoretical and experimental background for such combinations are currently being elucidated. << Less

  Drugs 34:372-390(1987) [PubMed] [EuropePMC]