Roles of The N- and C- Terminal Pro-Sequences of Aqualysin I Precursor in the Processing and Extracellular Secretion of the Enzyme

  • Young-Choon Lee
  • Ichiro Terada
  • Takahisa Ohta
  • Hiroshi Matsuzawa
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 379)


Aqualysin I is a subtilisin-type, heat-stable protease, which is secreted extracellularly by Thermus aquaticus YT-1, an extremely thermophilic, Gram-negative bacterium1–3. The enzyme contains two disulfide bonds4, which seem to be the cause of its heat stability. Aqualysin I is produced as a large precursor consisting of four structurally distinguishable domains; an N-terminal signal peptide (14 amino acid residues), an N-terminal pro-sequence (113 residues), the protease domain (281 residues) and a C-terminal pro-sequence (105 residues)5.


Outer Membrane Proteolytic Activity Cytoplasmic Membrane Protease Domain Mature Enzyme 
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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Young-Choon Lee
    • 1
  • Ichiro Terada
    • 1
  • Takahisa Ohta
    • 1
  • Hiroshi Matsuzawa
    • 1
  1. 1.Department of Agricultural ChemistryThe University of TokyoTokyoJapan

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