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

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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 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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Journal

Journal ID (iso-abbrev): Arch. Microbiol.

Title: Archives of microbiology

ISSN: 0302-8933

ISSN (Print): 0302-8933

Publication date (Electronic): Dec 1997

Volume: 168

Issue: 6

Affiliations

[1 ] Department of Microbiology, University of Bergen, Norway.

Article

PubMed ID: 9385147

SO-VID: c848850d-68ca-4c09-aa1e-e336d287e673

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