Isolation and characterization of two cDNAs from atlantic cod encoding two distinct psychrophilic elastases |
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Authors: | Elín Gudmundsdóttir Rémi Spilliaert Qing Yang Charles S Craik Jón B Bjarnason Agusta Gudmundsdóttir |
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Institution: | ∗Science Institute, University of Iceland, Dunhaga 3, 107 Reykjavik, Iceland;†Department of Pharmaceutical Chemistry, University of California, 513 Parnassus Avenue, San Francisco, CA, 94143-0446 USA |
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Abstract: | The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50–64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes. |
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Keywords: | Elastase serine protease psychrophilic cDNA sequence Atlantic cod |
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