Purification and properties of an extremely thermostable NADP+-specific glutamate dehydrogenase from Archaeoglobus fulgidus |
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| Authors: | Nina Aalén Ida Helene Steen Nils-Kåre Birkeland Torleiv Lien |
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| Affiliation: | (1) Department of Microbiology, University of Bergen, Jahnebakken 5, N-5020 Bergen, Norway Tel.: +47-55-582657; Fax +47-55-589671 e-mail: nils.birkeland@im.uib.no, NO;(2) Department of Microbiology, University of Bergen, Jahnebakken 5, N-5020 Bergen, Norway Tel.: +47-55-582657; Fax +47-55-589671 e-mail: nils.birkeland@im.uib.no, NO |
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| Abstract: | NADP+-specific glutamate dehydrogenase (EC 1.4.1.4) was purified to homogeneity from the extremely thermophilic, strictly anaerobic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324. The native enzyme (263 kDa) is composed of subunits of mol. mass 46 kDa, suggesting a hexameric structure. The temperature optimum for enzyme activity was > 95° C. The enzyme was highly thermostable, having a half-life of 140 min at 100° C. Potassium phosphate, KCl, and NaCl enhanced the thermal stability and increased the rate of activity three- to fourfold. The N-terminal 26-amino-acid sequence showed a high degree of similarity to glutamate dehydrogenases from Pyrococcus spp. and Thermococcus spp. Received: 25 March 1997 / Accepted: 11 July 1997 |
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| Keywords: | Archaeoglobus fulgidus Archaea Glutamate dehydrogenase Thermostable enzyme Amino acid dehydrogenase |
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