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Literature summary for 3.4.21.2 extracted from

  • Szmola, R.; Sahin-Toth, M.
    Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknechts enzyme Y (2007), Proc. Natl. Acad. Sci. USA, 104, 11227-11232.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ increasing the Ca2+ concentration from 0.025 mM to 1 mM progressively inhibits the degradation of cationic trypsin by chymotrypsin C, with essentially complete protection observed at 1 mM Ca2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99895
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cationic trypsin + H2O
-
Homo sapiens ? selectively cleaves the Leu81-Glu82 peptide bond within the Ca2-binding loop ?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
-
Homo sapiens N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
?
Trypsinogen + H2O
-
Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
caldecrin
-
Homo sapiens
enzyme Y chymotrypsin C is identical to enzyme Y, the trypsinogen-degrading enzymatic activity isolated from human pancreatic juice Homo sapiens