Information on EC 3.4.21.2 - chymotrypsin C

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
3.4.21.2
-
RECOMMENDED NAME
GeneOntology No.
chymotrypsin C
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage: Leu-/-, Tyr-/-, Phe-/-, Met-/-, Trp-/-, Gln-/-, Asn-/-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
caldecrin
-
-
caldecrin
Q99895
-
chymotrypsin C
-
-
chymotrypsinogen C
-
-
elastase-associated acidic endopeptidase
-
-
elastase-like chymotrypsin
-
-
enzyme Y
Q99895
chymotrypsin C is identical to enzyme Y, the trypsinogen-degrading enzymatic activity isolated from human pancreatic juice
Granzyme M
-
-
GrzM
-
-
Serum calcium-decreasing factor
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9036-09-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
pancreatitis-associated CTRC mutations can markedly increase the propensity of chymotrypsinogen C to elicit endoplasmic reticulum stress in pancreatic acinar cells. Diminished secretion and intracellular retention/degradation of the p.A73T CTRC mutant. Endoplasmic reticulum stress in AR42J cells is proportional to intracellular levels of the p.A73T CTRC mutant. No activation of the PERK pathway and NFkappaB in acinar cells expressing the p.A73T CTRC mutant. Apoptotic cell death in AR42J cells expressing the p.A73T CTRC mutant
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
A chain of oxidized insulin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Leu methyl ester + H2O
acetyl-L-Leu + methanol
show the reaction diagram
-
-
-
-
?
acetyl-L-Trp ethyl ester + H2O
acetyl-L-Trp + ethanol
show the reaction diagram
-
-
-
-
-
acetyl-L-Trp ethyl ester + H2O
acetyl-L-Trp + ethanol
show the reaction diagram
-
-
-
-
?
B chain of oxidized insulin + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-L-Leu methyl ester + H2O
benzoyl-L-Leu + methanol
show the reaction diagram
-
-
-
-
?
benzoyl-L-Met ethyl ester + H2O
benzoyl-L-Met + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-L-Tyr ethyl ester + H2O
benzoyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-Leu-ethyl ester + H2O
benzoyl-Leu + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-Phe ethyl ester + H2O
benzoyl-Phe + ethanol
show the reaction diagram
-
-
-
-
-
benzoyl-Phe ethyl ester + H2O
benzoyl-Phe + ethanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Leu-Gly-amide + H2O
benzyloxycarbonyl-L-Leu-Gly + NH3
show the reaction diagram
-
-
-
-
?
carboxymethylated reduced ribonuclease + H2O
?
show the reaction diagram
-
-
-
-
?
cationic trypsin + H2O
?
show the reaction diagram
-, Q99895
-
selectively cleaves the Leu81-Glu82 peptide bond within the Ca2-binding loop
-
?
cationic trypsinogen + H2O
?
show the reaction diagram
-
chymotrypsin activates trypsinogen by cleaving the N-terminal tripeptide of the protein
-
-
-
cationic trypsinogen A16V + H2O
?
show the reaction diagram
-
the A16V mutation of trypsinogen is processed 4fold more rapidly compared to wild-type trypsiongen
-
-
-
N-acetyl-Tyr ethyl ester + H2O
N-acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
Q99895
-
-
-
?
N-succinyl-L-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
oxidized oxytocin + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
Ser-His-Leu-Val-Glu + H2O
?
show the reaction diagram
-
-
-
-
?
Trypsinogen + H2O
?
show the reaction diagram
-, Q99895
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
hydrolysis of Tyr, Phe, Met, Trp, Leu, Glu, and Asp
-
-
-
additional information
?
-
-
no activity with N-benzoyl-L-Tyr-p-nitroanilide, L-Leu-p-nitroanilide, and N-benzoyl-L-Arg-p-nitroanilide
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
Q99895
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+
diphenyl carbamoyl chloride
-
-
tosyl-L-Leu chloromethyl ketone
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
acetyl-L-Leu methyl ester
-
-
2.1
-
acetyl-L-Trp ethyl ester
-
-
13
-
Acetyl-Tyr ethyl ester
-
-
28
-
benzoyl-L-Leu ethyl ester
-
-
0.4
-
benzoyl-L-Leu methyl ester
-
-
10
-
benzoyl-L-Met ethyl ester
-
-
17
-
benzoyl-L-Met ethyl ester
-
-
0.85
-
benzoyl-L-Phe ethyl ester
-
-
2
-
benzoyl-L-Tyr ethyl ester
-
-
15
-
benzyloxycarbonyl-L-Leu-Gly-amide
-
-
20
-
N-Acetyl-Tyr ethyl ester
-
-
0.000168
-
N-succinyl-L-Ala-Ala-Pro-Leu-p-nitroanilide
-
in 50 mM Tris-HCl (pH 8.0), with 20 mM CaCl2, at 37°C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
50
-
acetyl-L-Leu methyl ester
-
-
0.32
-
acetyl-L-Trp ethyl ester
-
-
92
-
Acetyl-Tyr ethyl ester
-
-
25.4
-
benzoyl-L-Leu ethyl ester
-
-
28
-
benzoyl-L-Leu methyl ester
-
-
1.7
-
benzoyl-L-Met ethyl ester
-
-
1.55
-
benzoyl-L-Phe ethyl ester
-
-
46
-
benzoyl-L-Tyr ethyl ester
-
-
80
-
benzoyl-L-Tyr ethyl ester
-
-
0.013
-
benzyloxycarbonyl-L-Leu-Gly amide
-
-
170
-
N-Acetyl-Tyr ethyl ester
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity is first detected at 6-7 days of age, glucocorticoids stimulate the perinatal development of pancreatic enzymes
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72100
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 30000, SDS-PAGE
?
-
x * 31800, calculation from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
chymotrypsin C is formed from subunit II of procarboxypeptidase A by specific cleavage by trypsin of the first basic bond in the N-terminal region
proteolytic modification
-
zymogen: chymotrypsinogen C
proteolytic modification
-
activation involves the specific cleavage by trypsin of the first basic bond in the N-terminal region
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
when activation with enterokinase is carried out further inactivation and/or breakdown occurs
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
aprotinin-agarose column chromatography
-
from inclusion bodies
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNAs for the wild-type CTRC and the p.A73T mutant carrying a Glu-Glu epitope tag excised from pcDNA3.1(-)_CTRC expression plasmids with XhoI and EcoRI and subcloned into the VQ Ad5CMV shuttle vector under the control of a CMV promoter. Dexamethasone-differentiated AR42J rat acinar cells and freshly isolated mouse acini transfected with recombinant adenovirus carrying wild-type CTRC or the p.A73T pancreatitis-associated mutant
-
expressed in HEK293-T cells
-
expression in Escherichia coli Rosetta (DE3)
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in AR42J cells and mouse acini, CTRC is transiently expressed in its inactive zymogen form
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A73T
-
diminished activity
Q48R
-
mutant shows about 30% activity of the wild type enzyme
R254W
-
shows about 50% of wild-type activity
R37Q
-
mutant shows essentially normal activity and secretion (about 82-88% activity of the wild type enzyme)
V235I
-
CTRC activity secreted by cells transfected with variant V235I is moderately reduced (about 65% of the wild type enzyme)
G217S
-
specific activity is about 7% of the wild type enzyme
additional information
-
deletion mutant K247_R254del shows diminished activity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
carriers of CTRC mutations may be at a higher risk of developing endoplasmic reticulum stress in the exocrine pancreas. Endoplasmic reticulum stress may contribute to parenchymal damage in chronic pancreatitis through acinar cell apoptosis