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Literature summary extracted from

  • Unger, W.G.; Watkins, J.; Stamford, I.F.
    Degradation of human serum albumin by human pepsins (1969), Biochem. J., 113, 8p-9p.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.2 Proteins + H2O Sus scrofa enzyme formed from pepsinogen B, more restricted specificity than pepsin A ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.2 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.2 proteolytic modification
-
 Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.23.2 degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe mechanism, concerted action of different pepsins Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.23.2 gastric juice
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.2 human serum albumin + H2O
-
 Sus scrofa ? + ?
-
 ir
3.4.23.2 proteins + H2O more restricted specificity than pepsin A Sus scrofa acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
-
 ir
3.4.23.2 Proteins + H2O enzyme formed from pepsinogen B, more restricted specificity than pepsin A Sus scrofa ?
-
 ?

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.23.2 2 3.4
-
 Sus scrofa