Literature summary for 3.4.22.53 extracted from

Masumoto, H.; Yoshizawa, T.; Sorimachi, H.; Nishino, T.; Ishiura, S.; Suzuki, K.
Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system (1998), J. Biochem., 124, 957-961.

Search for more literature for 3.4.22.53

Cloned(Commentary)

Cloned (Comment)	Organism
m-calpain is produced in a soluble form using a baculovirus expression system	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C105S	mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	0.4 mM Ca2+ is required for 50% caseinolysis of recombinant enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
casein + H2O	-	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)