Literature summary 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.

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.4.23.4	36000	-	? * 36000, SDS-PAGE, similar enzyme	Felis catus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.23.4	Felis catus	-	similar enzyme	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.4.23.4	similar enzyme	Felis catus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.4.23.4	gastric mucosa	-	Felis catus	-

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.4.23.4	2.5	-	-	Felis catus

pH Range

EC Number	pH Minimum	pH Maximum	Comment	Organism
3.4.23.4	1	5	acid-denatured hemoglobin, pH 1: about 80% of maximum activity, pH 5: about 30% of maximum activity	Felis catus

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Release 2023.1 (January 2023)