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Literature summary for 3.4.23.4 extracted from

  • Jensen, T.; Axelsen, N.H.; Foltmann, B.
    Isolation and partial characterization of prochymosin and chymosin from cat (1982), Biochim. Biophys. Acta, 705, 249-256.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
? * 36000, SDS-PAGE, similar enzyme Felis catus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
kappa-casein + H2O Felis catus cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106 ?
-
?

Organism

Organism UniProt Comment Textmining
Felis catus
-
similar enzyme
-

Purification (Commentary)

Purification (Comment) Organism
similar enzyme Felis catus

Source Tissue

Source Tissue Comment Organism Textmining
gastric mucosa
-
Felis catus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acid denatured hemoglobin + H2O
-
Felis catus ?
-
?
kappa-casein + H2O cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106 Felis catus p-kappa-casein + glycomacropeptide
-
?
kappa-casein + H2O cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106 Felis catus ?
-
?

Subunits

Subunits Comment Organism
More ? * 36000, SDS-PAGE, similar enzyme Felis catus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5
-
-
Felis catus

pH Range

pH Minimum pH Maximum Comment Organism
1 5 acid-denatured hemoglobin, pH 1: about 80% of maximum activity, pH 5: about 30% of maximum activity Felis catus