Immobilization–stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus

  title={Immobilization–stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus},
  author={Juan M. Bol{\'i}var and Felipe Cava and C. Gar{\'c}ia Mateo and Javier Rocha-Martin and Jos{\'e} M Guis{\'a}n and Jos{\'e} Berenguer and Roberto Fernandez-Lafuente},
  journal={Applied Microbiology and Biotechnology},
The genome of Thermus thermophilus contains two genes encoding putative glutamate dehydrogenases. One of these genes (TTC1211) was cloned and overexpressed in Escherichia coli. The purified enzyme was a trimer that catalyzed the oxidation of glutamate to α-ketoglutarate and ammonia with either NAD+ or NADP+ as cofactors. The enzyme was also able to catalyze the inverse reductive reaction. The thermostability of the enzyme at neutral pH was very high even at 70°C, but at acidic pH values, the… CONTINUE READING
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Thermostable glutamate dehydrogenase from a commensal thermophile, Symbiobacterium toebii overproduction, characterization, and application

  • JS Ha, K Kim, +6 authors MH Sung
  • J Mol Catal B: Enzym
  • 2003
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NAD - specific glutamate dehydrogenase from Thermus thermophilus HB 8 : purification and enzymatic properties

  • JL Ruiz, J Ferrer, BoneteM CamachoM
  • FEMS Microbiol Lett
  • 1998
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Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution

  • S Knapp, WM de Vos, D Rice, R Ladenstein
  • J Mol Biol
  • 1997
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Purification and properties of an extremely thermostable NADP+-specific glutamate dehydrogenase from Archaeoglobus fulgidus

  • N Alen, IH Steen, N-K Birkeland, T Lien
  • Arch Microbiol
  • 1997
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