ISSN:
1432-072X
Keywords:
Key words Archaeoglobus fulgidus
;
Archaea
;
Glutamate dehydrogenase
;
Thermostable enzyme
;
Amino acid dehydrogenase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050533
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