Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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