Purification and properties of an extremely thermostable NADP+-specific glutamate dehydrogenase from Archaeoglobus fulgidus

被引：18
作者：
Aalén, N [1 ]
Steen, IH [1 ]
Birkeland, NK [1 ]
Lien, T [1 ]
机构：
[1] Univ Bergen, Dept Microbiol, N-5020 Bergen, Norway
来源：
ARCHIVES OF MICROBIOLOGY | 1997年 / 168卷 / 06期
关键词：
Archaeoglobus fulgidus; archaea; glutamate dehydrogenase; thermostable enzyme; amino acid dehydrogenase;
D O I：
10.1007/s002030050533
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 degrees C. The enzyme was highly thermostable, having a half-life of 140 min at 100 degrees 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.
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收藏
页码：536 / 539
页数：4
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