Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases.
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.
Gudmundsdóttir
E
E
Science Institute, University of Iceland, Dunhaga, Reykjavik, Iceland.
Spilliaert
R
R
Yang
Q
Q
Craik
C S
CS
Bjarnason
J B
JB
Gudmundsdóttir
A
A
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003080:Cold Temperature; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification*; D005399:Fishes / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000235:genetics*; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000235:genetics*; D021382:Protein Sorting Signals / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D018076:DNA, Complementary; D007527:Isoenzymes; D021382:Protein Sorting Signals; D010196:Pancreatic Elastase