[11] Aldehyde Oxidoreductases from Pyrococcus furiosus
An early study with Pyrococcus furiosus showed that growth of this hyperthermophilic archaeon is stimulated by the addition of tungsten to the medium. Subsequently, three distinct tungsten-containing enzymes were purified from this and related organisms. They are aldehyde ferredoxin oxidoreductase (...
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| Veröffentlicht in: | Methods in Enzymology 2001, Vol.331, p.132-144 |
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| creator | Roy, Roopali Menon, Angeli L. Adams, Michael W.W. |
| description | An early study with Pyrococcus furiosus showed that growth of this hyperthermophilic archaeon is stimulated by the addition of tungsten to the medium. Subsequently, three distinct tungsten-containing enzymes were purified from this and related organisms. They are aldehyde ferredoxin oxidoreductase (AOR), which has been purifed from P. furiosus, Pyrococcus strain ES-4, and Thermococcus strain ES-1, formaldehyde ferredoxin oxidoreductase (FOR), which has been purified from Thermococcus litoralis and P. furiosus, 6 and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), which has been obtained so far only from P. furiosus. All three enzymes catalyze the oxidation of various types of aldehyde using ferredoxin (Fd) as the physiological electron acceptor. This chapter describes the purification of AOR, FOR, and GAPOR from P. furiosus and summarizes some of their properties. |
| doi_str_mv | 10.1016/S0076-6879(01)31052-2 |
| format | Article |
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Subsequently, three distinct tungsten-containing enzymes were purified from this and related organisms. They are aldehyde ferredoxin oxidoreductase (AOR), which has been purifed from P. furiosus, Pyrococcus strain ES-4, and Thermococcus strain ES-1, formaldehyde ferredoxin oxidoreductase (FOR), which has been purified from Thermococcus litoralis and P. furiosus, 6 and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), which has been obtained so far only from P. furiosus. All three enzymes catalyze the oxidation of various types of aldehyde using ferredoxin (Fd) as the physiological electron acceptor. 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Subsequently, three distinct tungsten-containing enzymes were purified from this and related organisms. They are aldehyde ferredoxin oxidoreductase (AOR), which has been purifed from P. furiosus, Pyrococcus strain ES-4, and Thermococcus strain ES-1, formaldehyde ferredoxin oxidoreductase (FOR), which has been purified from Thermococcus litoralis and P. furiosus, 6 and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), which has been obtained so far only from P. furiosus. All three enzymes catalyze the oxidation of various types of aldehyde using ferredoxin (Fd) as the physiological electron acceptor. This chapter describes the purification of AOR, FOR, and GAPOR from P. furiosus and summarizes some of their properties.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>11265456</pmid><doi>10.1016/S0076-6879(01)31052-2</doi><tpages>13</tpages></addata></record> |
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| subjects | Aldehyde Oxidoreductases - chemistry Aldehyde Oxidoreductases - isolation & purification Aldehyde Oxidoreductases - metabolism Chromatography - methods Chromatography, Ion Exchange - methods Durapatite Enzyme Stability Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry Glyceraldehyde-3-Phosphate Dehydrogenases - isolation & purification Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Hot Temperature Kinetics Metals - analysis Protein Subunits Pyrococcus furiosus - enzymology Pyrococcus furiosus - growth & development Substrate Specificity Thermodynamics |
| title | [11] Aldehyde Oxidoreductases from Pyrococcus furiosus |
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