Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway inSulfolobus solfataricus
| Autor: | Garry L. Taylor, Christine C. Milburn, Michael J. Danson, David W. Hough, Henry J. Lamble |
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| Rok vydání: | 2004 |
| Předmět: |
Cell Extracts
Entner–Doudoroff pathway Galactonate dehydratase ved/biology.organism_classification_rank.species Biophysics Biology Biochemistry Catalysis Substrate Specificity Sulfolobus chemistry.chemical_compound Structural Biology Glucose dehydrogenase Enzyme Stability Genetics Gluconate dehydratase Amino Acid Sequence Molecular Biology Hydro-Lyases chemistry.chemical_classification Metabolic pathway promiscuity ved/biology Sulfolobus solfataricus Aldolase A Temperature Cell Biology Chromatography Ion Exchange Archaea Molecular Weight Kinetics Enzyme chemistry Genes Bacterial Galactose Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Half-Life |
| Zdroj: | FEBS Letters. 576:133-136 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2004.08.074 |
| Popis: | An investigation has been carried out into gluconate dehydratase from the hyperthermophilic Archaeon Sulfolobus solfataricus. The enzyme has been purified from cell extracts of the organism and found to be responsible for both gluconate and galactonate dehydratase activities. It was shown to be a 45 kDa monomer with a half-life of 41 min at 95 °C and it exhibited similar catalytic efficiency with both substrates. Taken alongside the recent work on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase, this report clearly demonstrates that the entire non-phosphorylative Entner–Doudoroff pathway of S. solfataricus is promiscuous for the metabolism of both glucose and galactose. |
| Databáze: | OpenAIRE |
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