Literature summary for 3.4.21.39 extracted from

Pejler, G.; Berg, L.
Regulation of rat mast cell protease 1 activity. Protease inhibition is prevented by heparin proteoglycan (1995), Eur. J. Biochem., 233, 192-199.

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Inhibitors

Inhibitors	Comment	Organism	Structure
alpha1-Aantichymotrypsin	native chymase-heparin proteoglycan complex is largely resistant to inhibition by alpha1-antichymotrypsin	Rattus norvegicus
additional information	endogenous mast cell heparin proteoglycan significantly blocks the inhibition of the enzyme by the serpins alpha1-protease inhibitor and alpha1-antichymotrypsin as well as the inhibition by alpha2-macroglobulin, soybean trypsin inhibitor and plasma. Native chymase-heparin proteoglycan complex is largely resistant to inhibition by alpha1-antichymotrypsin and alpha1-protease inhibitor	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.3	-	methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide	in presence of heparin proteoglycan	Rattus norvegicus
1.8	-	methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide	in absence of heparin	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	the association of the enzyme with heparin proteoglycan may serve both to potentiate the catalytic activity of the enzyme and to increase the life-span of the chymase by preventing their inhibition after exocytosis	Rattus norvegicus	-	-
secretory granule	-	Rattus norvegicus	30141	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
mast cell	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O	-	Rattus norvegicus	methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline	-	?

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Release 2023.1 (January 2023)