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Applied Microbiology and Biotechnology

, Volume 56, Issue 3–4, pp 388–394 | Cite as

Characterization of native glutamate dehydrogenase from an aerobic hyperthermophilic archaeon Aeropyrum pernix K1

  •  I. Helianti
  •  Y. Morita
  •  A. Yamamura
  •  Y. Murakami
  •  K. Yokoyama
  •  E. Tamiya
Original Paper

Abstract.

Glutamate dehydrogenase (GDH) was purified and characterized from an aerobic hyperthermophilic archaeon Aeropyrum pernix (A. pernix) K1. The enzyme has a hexameric structure with a native molecular mass of about 285±15 kDa. It was specific for NADP and thermostable (74% activity was remained after 5 h incubation at 100 °C). The activity of the enzyme increased in the presence of polar water-miscible organic solvents such as acetonitrile, methanol, and ethanol. The N-terminal sequence of GDH is Met-Gln-Pro-Thr-Asp-Pro-Leu-Glu-Glu-Ala. This sequence, except for the methionine, corresponds to amino acids 7–15 of the open reading frame (ORF) encoding the predicted GDH (ORF APE 1386). In the ORF nucleotide sequence, the codon TTG appears at the position of the methionine, suggesting that the leucine codon might be recognized as an initiation codon and translated to methionine in A. pernix GDH.

Keywords

Enzyme Nucleotide Codon Glutamate Acetonitrile 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  •  I. Helianti
    • 1
  •  Y. Morita
    • 1
  •  A. Yamamura
    • 1
  •  Y. Murakami
    • 1
  •  K. Yokoyama
    • 1
  •  E. Tamiya
    • 1
  1. 1.School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan

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