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Literature summary for 3.4.21.B3 extracted from

  • Mirgorodskaya, O.; Kazanina, G.; Mirgorodskaya, E.; Vorotyntseva, T.; Zamolodchikova, T.; Alexandrov, S.
    A comparative study of the specificity of melittin hydrolysis by duodenase, trypsin and plasmin (1996), Protein Pept. Lett., 3, 315-320.
No PubMed abstract available
Search for more literature for 3.4.21.B3

Application

Application Comment Organism
analysis comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in analytical protein chemistry Bos taurus
biotechnology comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in biotechnology Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
polypeptide + H2O Bos taurus enzyme belongs to the serine protease subfamily peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus P80219
-
-

Reaction

Reaction Comment Organism Reaction ID
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro active site serine Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
duodenum exclusive Bos taurus
-
mucosa
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
melittin + H2O leaved sites, specificity, overview Bos taurus fragments of melittin
-
 ?
polypeptide + H2O
-
 Bos taurus peptides
-
 ?
polypeptide + H2O enzyme belongs to the serine protease subfamily Bos taurus peptides
-
 ?

Synonyms

Synonyms Comment Organism
duodenase I
-
 Bos taurus
duodenase serine protease
-
 Bos taurus