Literature summary for 3.4.21.59 extracted from

Yoshida, N.; Everitt, M.T.; Neurath, H.; Woodbury, R.G.; Powers, J.C.
Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G (1980), Biochemistry, 19, 5799-5804.

Search for more literature for 3.4.21.59

Inhibitors

Inhibitors	Comment	Organism	Structure
Peptide chloromethyl ketone inhibitors	-	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	overview: Km values of peptide 4-nitroanilide substrates	Rattus norvegicus

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.
additional information	specificity overview: peptide 4-nitroanilides	Rattus norvegicus	?	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	of peptide 4-nitroanilide substrates	Rattus norvegicus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)