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Applied Microbiology and Biotechnology

, Volume 59, Issue 4–5, pp 462–466 | Cite as

Expression of two kinds of recombinant glutamate dehydrogenase from Aeropyrum pernix with different N-terminal sequence length in Escherichia coli

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

Abstract.

Two recombinant Aeropyrum pernix glutamate dehydrogenase (GDH) enzymes with different length N-termini were cloned and expressed in Escherichia coli: sGDH begins with the amino acid sequence of the extracted native enzyme (M-Q-P-T-D-P-L-E-E), whereas lGDH begins with the sequence of the predicted ORF (M-E-V-L-A-L-Q-P-T-D) and is longer than sGDH by five amino acids (M-E-V-L-A). Purified recombinant lGDH was more stable than sGDH, indicating that the N-terminal extension, containing mostly hydrophobic residues, affected the overall stability of recombinant lGDH. This stabilising effect of extending the N-terminal sequence on an oligomeric enzyme such as GDH is novel; factors affecting stabilisation have previously only been discussed in the context of the contribution of internal amino acids.

Keywords

Enzyme Escherichia Coli Glutamate Amino Acid Sequence Sequence Length 
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 2002

Authors and Affiliations

  •  I. Helianti
    • 1
  •  Y. Morita
    • 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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