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Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation
Genicot, S.; Rentier-Delrue, F.; Edwards, D.; Van Beeumen, J.; Gerday, C. (1996). Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1298(1): 45-57. dx.doi.org/10.1016/S0167-4838(96)00095-7
In: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Elsevier: Amsterdam. ISSN 1878-1454, more
Peer reviewed article  

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Keywords
    Paranotothenia magellanica (Forster, 1801) [WoRMS]; Marine
Author keywords
    trypsin; cold adaptation; Antarctic fish; three-dimensional structure;(P-magellanica)

Authors  Top 
  • Genicot, S.
  • Rentier-Delrue, F.
  • Edwards, D.
  • Van Beeumen, J.
  • Gerday, C., more

Abstract
    Trypsin from Antarctic fish Paranotothenia magellanica displays molecular and kinetic properties typical of enzymes produced by psychrophilic organisms. The enzyme has a high catalytic efficiency at low and moderate temperatures and is rapidly inactivated at temperatures higher than 30°C. The nucleotide sequence was determined after mRNA extraction and cDNA synthesis. The cDNA encodes a pretrypsinogen which includes a seven residue activation peptide containing only three acidic residues preceeding the 222 amino-acid mature enzyme. A three-dimensional model of the enzyme was built. Structural parameters possibly involved in the adaptation to cold have been derived from comparison with the three-dimensional structure of the bovine enzyme. Among them are the lack of Tyr-151 in the substrate binding pocket, an overall decrease in the number of salt bridges and hydrophobicity and the increase in the surface hydrophilicity.

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