3.4.21.2: chymotrypsin C
This is an abbreviated version!
For detailed information about chymotrypsin C, go to the full flat file.
Reaction
Preferential cleavage: Leu-/-, Tyr-/-, Phe-/-, Met-/-, Trp-/-, Gln-/-, Asn-/- =
Synonyms
caldecrin, chymotrypsin C, chymotrypsinogen C, CTRC, elastase-associated acidic endopeptidase, elastase-like chymotrypsin, enzyme Y, Granzyme M, GrzM, Serum calcium-decreasing factor
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.2 - chymotrypsin C
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REACTION DIAGRAM
benzyloxycarbonyl-L-Leu-Gly-amide + H2O
benzyloxycarbonyl-L-Leu-Gly + NH3
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-
-
-
?
cationic trypsin + H2O
?
-
selectively cleaves the Leu81-Glu82 peptide bond within the Ca2-binding loop
-
?
cationic trypsinogen + H2O
?
-
chymotrypsin activates trypsinogen by cleaving the N-terminal tripeptide of the protein
-
-
?
cationic trypsinogen A16V + H2O
?
-
the A16V mutation of trypsinogen is processed 4fold more rapidly compared to wild-type trypsiongen
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
N-succinyl-L-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Ala 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Ala + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Asn 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Asn + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Gln 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Gln + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Ile 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Ile + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Leu 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Met 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Trp 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Trp + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Tyr 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Tyr + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Val 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
?
human cationic trypsinogen + H2O
?
-
enzyme cleaves the Leu81-Glu82 peptide bond in the calcium-binding loop. Chymotrypsin C-mediated cleavage is stimulated threefold by mutation E82A and unaffected by mutations E79A and N84A in human cationic trypsinogen. Specific cleavage of the Leu81-Glu82 peptide bond is primarily determined by the enzymes' distinctively high activity on leucyl peptide bonds, with the P1' Glu82, P3' Asn84 and P4' Glu85 residues serving as additional specificity determinants
-
?
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Trypsinogen + H2O
?
chymotrypsin C protects against pancreatitis by degrading trypsinogen and thereby curtailing harmful intrapancreatic trypsinogen activation
-
-
?
?
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-
no activity with N-benzoyl-L-Tyr-p-nitroanilide, L-Leu-p-nitroanilide, and N-benzoyl-L-Arg-p-nitroanilide
-
-
?
additional information
?
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CTRC cleaves after a P1 Leu with at least tenfold higher catalytic efficiency than other enzymes tested
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-
?
additional information
?
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-
CTRC cleaves after a P1 Leu with at least tenfold higher catalytic efficiency than other enzymes tested
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-
?
additional information
?
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-
hydrolysis of Tyr, Phe, Met, Trp, Leu, Glu, and Asp
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-
?