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Literature summary for 3.4.23.2 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
Search for more literature for 3.4.23.2

Activating Compound

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification
-
 Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
mucosa
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
-
 Sus scrofa