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Literature summary extracted from

  • Nielsen, P.K.; Foltmann, B.
    Purification and characterization of porcine pepsinogen B and pepsin B (1995), Arch. Biochem. Biophys., 322, 417-422.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.23.2 additional information mechanism of activation Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.2 39000
-
 SDS-PAGE Sus scrofa
3.4.23.2 40000
-
 SDS-PAGE, pepsinogen B Sus scrofa

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.2
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.23.2 mucosa
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.23.2 additional information
-
 modified Anson test Sus scrofa

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.4.23.2 ? x * 39000, SDS-PAGE Sus scrofa
3.4.23.2 ? N-terminal amino acid sequence reported Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.2 3
-
-
 Sus scrofa