Literature summary for 3.4.21.4 extracted from
Kanno, G.; Kishimura, H.; Ando, S.; Klomklao, S.; Nalinanon, S.; Benjakul, S.; Chun, B.; Saeki, H.
Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus) (2011), Eur. Food Res. Technol., 232, 381-388.
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
a cDNA clone encoding trypsin is isolated from the pyloric ceca of cold-adapted fish, DNA and amino acid sequence determination and analysis, sequence comparisons with the Bos taurus enzyme, differences in Y151del and G152P of the autolysis loop |
Pleurogrammus azonus |
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Ca2+ |
required, amino acid residues Glu70, Asn72, Glu77, and Glu80 are conserved in the calcium-binding loop |
Pleurogrammus azonus |
|
Natural Substrates/ Products (Substrates)
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
additional information |
Pleurogrammus azonus |
trypsin specifically cleaves the peptide bond on the carboxyl side of Lys and Arg residues. It is characterized by a common catalytic mechanism involving the catalytic triad of three essential amino acid residues His57, Asp102, and Ser195 and a substrate determinant residue Asp189 |
? |
- |
? |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Pleurogrammus azonus |
B3IYE4 |
- |
- |
Source Tissue
Source Tissue |
Comment |
Organism |
Textmining |
cecum |
pyloric |
Pleurogrammus azonus |
- |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
additional information |
trypsin specifically cleaves the peptide bond on the carboxyl side of Lys and Arg residues. It is characterized by a common catalytic mechanism involving the catalytic triad of three essential amino acid residues His57, Asp102, and Ser195 and a substrate determinant residue Asp189 |
Pleurogrammus azonus |
? |
- |
? |
|
Synonyms
Synonyms |
Comment |
Organism |
More |
trypsin is a member of the large family of serine proteases |
Pleurogrammus azonus |
General Information
General Information |
Comment |
Organism |
additional information |
completely conserved major structural features common to trypsin such as the catalytic triad, formed by His57, Asp102, and Ser195, the obligatory Asp189 and twelve Cys residues, but with deletion of Tyr151 and substitution of Pro152 for Gly in the autolysis loop |
Pleurogrammus azonus |
physiological function |
trypsin is a major digestive enzyme |
Pleurogrammus azonus |