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A chain of oxidized insulin + H2O
?
-
-
-
-
?
acetyl-L-Leu methyl ester + H2O
acetyl-L-Leu + methanol
-
-
-
-
?
acetyl-L-Trp ethyl ester + H2O
acetyl-L-Trp + ethanol
-
-
-
-
?
anionic trypsinogen + H2O
?
-
-
-
?
B chain of oxidized insulin + H2O
?
-
-
-
-
?
benzoyl-L-Leu methyl ester + H2O
benzoyl-L-Leu + methanol
-
-
-
-
?
benzoyl-L-Met ethyl ester + H2O
benzoyl-L-Met + ethanol
-
-
-
-
?
benzoyl-L-Tyr ethyl ester + H2O
benzoyl-L-Tyr + ethanol
-
-
-
-
?
benzoyl-Leu-ethyl ester + H2O
benzoyl-Leu + ethanol
-
-
-
-
?
benzoyl-Phe ethyl ester + H2O
benzoyl-Phe + ethanol
-
-
-
-
?
benzyloxycarbonyl-L-Leu-Gly-amide + H2O
benzyloxycarbonyl-L-Leu-Gly + NH3
-
-
-
-
?
beta-casein + H2O
?
-
-
-
?
carboxymethylated reduced ribonuclease + H2O
?
-
-
-
-
?
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
-
-
?
Glucagon + H2O
?
-
-
-
-
?
human cationic trypsinogen + H2O
?
N-acetyl-Tyr ethyl ester + H2O
N-acetyl-Tyr + ethanol
-
-
-
-
?
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
-
-
-
-
?
oxidized oxytocin + H2O
?
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
Ser-His-Leu-Val-Glu + H2O
?
-
-
-
-
?
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-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
-
-
-
?
additional information
?
-
human cationic trypsinogen + H2O
?
-
-
-
?
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-nitroanilide + H2O
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-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Trypsinogen + H2O
?
-
-
-
?
Trypsinogen + H2O
?
chymotrypsin C protects against pancreatitis by degrading trypsinogen and thereby curtailing harmful intrapancreatic trypsinogen activation
-
-
?
additional information
?
-
-
no activity with N-benzoyl-L-Tyr-p-nitroanilide, L-Leu-p-nitroanilide, and N-benzoyl-L-Arg-p-nitroanilide
-
-
?
additional information
?
-
CTRC cleaves after a P1 Leu with at least tenfold higher catalytic efficiency than other enzymes tested
-
-
?
additional information
?
-
-
CTRC cleaves after a P1 Leu with at least tenfold higher catalytic efficiency than other enzymes tested
-
-
?
additional information
?
-
-
hydrolysis of Tyr, Phe, Met, Trp, Leu, Glu, and Asp
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Bone Resorption
Caldecrin: A pancreas-derived hypocalcemic factor, regulates osteoclast formation and function.
Bone Resorption
Determination of amino acid sequence responsible for suppression of bone resorption by serum calcium-decreasing factor (caldecrin).
Bone Resorption
Purification and Biological Function of Caldecrin.
Bone Resorption
Rat brain expresses serum calcium-decreasing factor (caldecrin).
Bone Resorption
Serum calcium-decreasing factor, caldecrin, inhibits receptor activator of NF-?B ligand (RANKL)-mediated Ca2+ signaling and actin ring formation in mature osteoclasts via suppression of Src signaling pathway.
Cystic Fibrosis
CFTR, SPINK1, PRSS1, and CTRC Mutations Are Not Associated With Pancreatic Cancer in German Patients.
Cystic Fibrosis
Chronic pancreatitis associated with the p.G208A variant of PRSS1 gene in a European patient.
Cystic Fibrosis
Comprehensive screening for PRSS1, SPINK1, CFTR, CTRC and CLDN2 gene mutations in Chinese paediatric patients with idiopathic chronic pancreatitis: a cohort study.
Cystic Fibrosis
Environmental risk factors for chronic pancreatitis and pancreatic cancer.
Cystic Fibrosis
Genetic and phenotypic heterogeneity in tropical calcific pancreatitis.
Cystic Fibrosis
Genetic aspects of pancreatitis.
Cystic Fibrosis
Genetic Evaluation of Children with Idiopathic Recurrent Acute Pancreatitis.
Cystic Fibrosis
Genetics of acute and chronic pancreatitis: An update.
Cystic Fibrosis
Targeted Gene Next-Generation Sequencing in Chinese Children with Chronic Pancreatitis and Acute Recurrent Pancreatitis.
Cysts
Early-Onset Acute Recurrent and Chronic Pancreatitis Is Associated with PRSS1 or CTRC Gene Mutations.
Kidney Failure, Chronic
Early-Onset Acute Recurrent and Chronic Pancreatitis Is Associated with PRSS1 or CTRC Gene Mutations.
Muscular Dystrophies
Serum Calcium-decreasing Factor, Caldecrin, Ameliorates Muscular Dystrophy in dy/dy Mice.
Neoplasms
Effect of chymotrypsin C and related proteins on pancreatic cancer cell migration.
Osteoarthritis
Caldecrin: A pancreas-derived hypocalcemic factor, regulates osteoclast formation and function.
Osteoporosis
Caldecrin: A pancreas-derived hypocalcemic factor, regulates osteoclast formation and function.
Pancreatic Neoplasms
CFTR, SPINK1, PRSS1, and CTRC Mutations Are Not Associated With Pancreatic Cancer in German Patients.
Pancreatic Neoplasms
Effect of chymotrypsin C and related proteins on pancreatic cancer cell migration.
Pancreatitis
Chronic pancreatitis associated with the p.G208A variant of PRSS1 gene in a European patient.
Pancreatitis
Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen.
Pancreatitis
Comprehensive functional analysis of chymotrypsin C (CTRC) variants reveals distinct loss-of-function mechanisms associated with pancreatitis risk.
Pancreatitis
Comprehensive screening of chymotrypsin C (CTRC) gene in tropical calcific pancreatitis identifies novel variants.
Pancreatitis
Early-Onset Acute Recurrent and Chronic Pancreatitis Is Associated with PRSS1 or CTRC Gene Mutations.
Pancreatitis
Evaluation of the Pathogenic Significance of the Novel p.T58M Chymotrypsin C Variant in Recurrent Acute Pancreatitis.
Pancreatitis
Frequency of Tabagism and N34S and P55S Mutations of Serine Peptidase Inhibitor, Kazal Type 1 (SPINK1) and R254W Mutation of Chymotrypsin C (CTRC) in Patients With Chronic Pancreatitis and Controls.
Pancreatitis
Functional effects of 13 rare PRSS1 variants presumed to cause chronic pancreatitis.
Pancreatitis
Genetic basis of chronic pancreatitis in Asia Pacific region.
Pancreatitis
Genetic Evaluation of Children with Idiopathic Recurrent Acute Pancreatitis.
Pancreatitis
Genetics of pancreatitis: the 2014 update.
Pancreatitis
Mesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.
Pancreatitis
Multifactorial Genesis of Pancreatitis in Primary Hyperparathyroidism: Evidence for "Protective" (PRSS2) and "Destructive" (CTRC) Genetic Factors.
Pancreatitis
Natural single-nucleotide deletion in chymotrypsinogen C gene increases severity of secretagogue-induced pancreatitis in C57BL/6 mice.
Pancreatitis
Paediatric and hereditary aspects of chronic pancreatitis.
Pancreatitis
Relationship between CFTR and CTRC Variants and the Clinical Phenotype in Late-Onset Cystic Fibrosis Disease with Chronic Pancreatitis.
Pancreatitis
Robust autoactivation, chymotrypsin C independence and diminished secretion define a subset of hereditary pancreatitis-associated cationic trypsinogen mutants.
Pancreatitis
The Common Chymotrypsinogen C (CTRC) Variant G60G (C.180T) Increases Risk of Chronic Pancreatitis But Not Recurrent Acute Pancreatitis in a North American Population.
Pancreatitis
Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis.
Pancreatitis, Alcoholic
Frequency of Tabagism and N34S and P55S Mutations of Serine Peptidase Inhibitor, Kazal Type 1 (SPINK1) and R254W Mutation of Chymotrypsin C (CTRC) in Patients With Chronic Pancreatitis and Controls.
Pancreatitis, Chronic
Association of Novel Chymotrypsin C Gene Variations and Haplotypes in Patients with Chronic Pancreatitis in Chinese in Taiwan.
Pancreatitis, Chronic
Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis.
Pancreatitis, Chronic
CFTR, SPINK1, PRSS1, and CTRC Mutations Are Not Associated With Pancreatic Cancer in German Patients.
Pancreatitis, Chronic
Chronic pancreatitis associated with the p.G208A variant of PRSS1 gene in a European patient.
Pancreatitis, Chronic
Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis.
Pancreatitis, Chronic
Chymotrypsin C mutations in chronic pancreatitis.
Pancreatitis, Chronic
Chymotrypsinogen C Genetic Variants, Including c.180TT, Are Strongly Associated With Chronic Pancreatitis in Pediatric Patients.
Pancreatitis, Chronic
Clinical interpretation of SPINK1 and CTRC variants in pancreatitis.
Pancreatitis, Chronic
Comprehensive screening of chymotrypsin C (CTRC) gene in tropical calcific pancreatitis identifies novel variants.
Pancreatitis, Chronic
Frequency of Tabagism and N34S and P55S Mutations of Serine Peptidase Inhibitor, Kazal Type 1 (SPINK1) and R254W Mutation of Chymotrypsin C (CTRC) in Patients With Chronic Pancreatitis and Controls.
Pancreatitis, Chronic
Genetic aspects of pancreatitis.
Pancreatitis, Chronic
Genetic causes of chronic pancreatitis: the elucidation of genetic contributions to a disorder once thought to have none.
Pancreatitis, Chronic
Mesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.
Pancreatitis, Chronic
Molecular basis for pancreatitis.
Pancreatitis, Chronic
Mutational analysis of ATP8B1 in patients with chronic pancreatitis.
Pancreatitis, Chronic
Natural single-nucleotide deletion in chymotrypsinogen C gene increases severity of secretagogue-induced pancreatitis in C57BL/6 mice.
Pancreatitis, Chronic
Pancreatitis-associated chymotrypsinogen C (CTRC) mutant elicits endoplasmic reticulum stress in pancreatic acinar cells.
Pancreatitis, Chronic
The Common Chymotrypsinogen C (CTRC) Variant G60G (C.180T) Increases Risk of Chronic Pancreatitis But Not Recurrent Acute Pancreatitis in a North American Population.
Pancreatitis, Chronic
Tropical calcific pancreatitis and its association with CTRC and SPINK1 (p.N34S) variants.
Pancreatitis, Chronic
[Chronic pancreatitis]
Pulmonary Fibrosis
Serpina3n is closely associated with fibrotic procession and knockdown ameliorates bleomycin-induced pulmonary fibrosis.
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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 - 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
-
-
0.0105 - 0.0134
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
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
0.392
succinyl-Ala-Ala-Pro-Ala 4-nitroanilide
pH 8.0, temperature not specified in the publication
3.452
succinyl-Ala-Ala-Pro-Asn 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.738
succinyl-Ala-Ala-Pro-Gln 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.0605
succinyl-Ala-Ala-Pro-Ile 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.0118
succinyl-Ala-Ala-Pro-Leu 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.0304
succinyl-Ala-Ala-Pro-Met 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.013 - 1.539
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
0.0153 - 0.0472
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.0277
succinyl-Ala-Ala-Pro-Trp 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.0196
succinyl-Ala-Ala-Pro-Tyr 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.1504
succinyl-Ala-Ala-Pro-Val 4-nitroanilide
pH 8.0, temperature not specified in the publication
10
benzoyl-L-Met ethyl ester
-
-
17
benzoyl-L-Met ethyl ester
-
-
0.0105
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
mutant enzyme T58M, pH and temperature not specified in the publication
0.0134
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
wild-type enzyme, pH and temperature not specified in the publication
0.013
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
wild-type, pH 8.0, 22°C
0.015
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254Q, pH 8.0, 22°C
0.015
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254W, pH 8.0, 22°C
0.016
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q48R, pH 8.0, 22°C
0.016
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V235I, pH 8.0, 22°C
0.017
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant D35Y, pH 8.0, 22°C
0.017
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G18R, pH 8.0, 22°C
0.02
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R37Q, pH 8.0, 22°C
0.022
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.024
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant A73T, pH 8.0, 22°C
0.482
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G217S, pH 8.0, 22°C
0.495
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q178R, pH 8.0, 22°C
0.59
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G32V, pH 8.0, 22°C
0.761
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant P249L, pH 8.0, 22°C
1.539
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V250E, pH 8.0, 22°C
0.0153
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, wild-type enzyme
0.0157
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme I209M
0.0167
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme K247E
0.019
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239A
0.0194
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80W
0.0221
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214M
0.0221
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214R
0.0226
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80Q
0.0331
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239C
0.0472
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 - 80
benzoyl-L-Tyr ethyl ester
0.013
benzyloxycarbonyl-L-Leu-Gly amide
-
-
170
N-Acetyl-Tyr ethyl ester
-
-
11.7 - 24
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.3
succinyl-Ala-Ala-Pro-Ala 4-nitroanilide
pH 8.0, temperature not specified in the publication
3.6
succinyl-Ala-Ala-Pro-Asn 4-nitroanilide
pH 8.0, temperature not specified in the publication
1.1
succinyl-Ala-Ala-Pro-Gln 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.03
succinyl-Ala-Ala-Pro-Ile 4-nitroanilide
pH 8.0, temperature not specified in the publication
9.2
succinyl-Ala-Ala-Pro-Leu 4-nitroanilide
pH 8.0, temperature not specified in the publication
14.9
succinyl-Ala-Ala-Pro-Met 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.6 - 16.6
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
0.6 - 42.2
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.1
succinyl-Ala-Ala-Pro-Trp 4-nitroanilide
pH 8.0, temperature not specified in the publication
16.6
succinyl-Ala-Ala-Pro-Tyr 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.05
succinyl-Ala-Ala-Pro-Val 4-nitroanilide
pH 8.0, temperature not specified in the publication
46
benzoyl-L-Tyr ethyl ester
-
-
80
benzoyl-L-Tyr ethyl ester
-
-
11.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
wild-type enzyme, pH and temperature not specified in the publication
24
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
mutant enzyme T58M, pH and temperature not specified in the publication
0.6
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant P249L, pH 8.0, 22°C
1.4
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V250E, pH 8.0, 22°C
2.7
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G217S, pH 8.0, 22°C
3.5
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q178R, pH 8.0, 22°C
10
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G32V, pH 8.0, 22°C
11.7
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant D35Y, pH 8.0, 22°C
12.6
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V235I, pH 8.0, 22°C
13.2
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
pH 8.0, temperature not specified in the publication
14.4
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R37Q, pH 8.0, 22°C
15
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
wild-type, pH 8.0, 22°C
15.1
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q48R, pH 8.0, 22°C
15.5
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254Q, pH 8.0, 22°C
15.7
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G18R, pH 8.0, 22°C
16.6
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant A73T, pH 8.0, 22°C
16.6
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254W, pH 8.0, 22°C
0.6
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239C
10.3
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme I209M
11.7
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239A
14.1
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214A
14.7
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme K247E
15.1
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80W
15.4
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, wild-type enzyme
16.5
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80Q
23.6
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214M
42.2
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214R
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0.77
succinyl-Ala-Ala-Pro-Ala 4-nitroanilide
pH 8.0, temperature not specified in the publication
1
succinyl-Ala-Ala-Pro-Asn 4-nitroanilide
pH 8.0, temperature not specified in the publication
1.5
succinyl-Ala-Ala-Pro-Gln 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.5
succinyl-Ala-Ala-Pro-Ile 4-nitroanilide
pH 8.0, temperature not specified in the publication
780
succinyl-Ala-Ala-Pro-Leu 4-nitroanilide
pH 8.0, temperature not specified in the publication
490
succinyl-Ala-Ala-Pro-Met 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.79 - 1100
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
18 - 1900
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
3.6
succinyl-Ala-Ala-Pro-Trp 4-nitroanilide
pH 8.0, temperature not specified in the publication
850
succinyl-Ala-Ala-Pro-Tyr 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.33
succinyl-Ala-Ala-Pro-Val 4-nitroanilide
pH 8.0, temperature not specified in the publication
0.79
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant P249L, pH 8.0, 22°C
0.91
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V250E, pH 8.0, 22°C
5.5
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G217S, pH 8.0, 22°C
7.1
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q178R, pH 8.0, 22°C
17
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G32V, pH 8.0, 22°C
600
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
pH 8.0, temperature not specified in the publication
680
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant A73T, pH 8.0, 22°C
680
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant D35Y, pH 8.0, 22°C
710
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R37Q, pH 8.0, 22°C
800
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant V235I, pH 8.0, 22°C
920
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant G18R, pH 8.0, 22°C
930
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant Q48R, pH 8.0, 22°C
1000
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254Q, pH 8.0, 22°C
1100
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
wild-type, pH 8.0, 22°C
1100
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
mutant R254W, pH 8.0, 22°C
18
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239C
300
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214A
620
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme S239A
660
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme I209M
730
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80Q
780
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme R80W
880
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme K247E
1000
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, wild-type enzyme
1100
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214M
1900
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 22°C, mutant enzyme G214R
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D35Y
natural missense variant, 62% of wild-type activity
G18R
natural missense variant, 84% of wild-type activity
G214A
activity is similar to wild-type enzyme
G214M
activity is similar to wild-type enzyme
G214R
the mutant has increased activity on a small chromogenic peptide substrate but is markedly defective in cleaving bovine beta-casein or the natural chymotrypsin C substrates human cationic trypsinogen and procarboxypeptidase A1. Mutation p.G214R is analogous to the evolutionary mutation in human mesotrypsin, which renders this trypsin isoform resistant to proteinaceous inhibitors and conferrs its ability to cleave these inhibitors. Similarly to the mesotrypsin phenotype, chymotrypsin C variant p.G214R is inhibited poorly by eglin C, ecotin, or a chymotrypsin C-specific variant of SGPI-2, and it readily cleaves the reactive-site peptide bonds in eglin C and ecotin
G217R
natural missense variant, no residual activity
G32V
natural missense variant, 1.5% of wild-type activity
I209M
activity is similar to wild-type enzyme
K247-R254del
natural missense variant, no residual activity
K247E
activity is similar to wild-type enzyme
mre
None of the mutants examined exhibits a gain of function such as increased secretion or activity. 11 mutants show marked loss of function, 3 mutants have moderate functional defects, whereas 18 mutants are functionally similar to wild-type. The functional deficiencies observed are diminished secretion, impaired catalytic activity and degradation by trypsin. Mutants with a secretion defect cause ER stress that is proportional to the loss in secretion. ER stress is not associated with loss-of-function phenotypes related to catalytic defect or proteolytic instability
P249L
natural missense variant, 0.07% of wild-type activity
Q178R
natural missense variant, 0.6% of wild-type activity
R254Q
natural missense variant, 91% of wild-type activity
R29Q
catalytically inactive due to loss of activation by trypsin
R80Q
activity is similar to wild-type enzyme
R80W
activity is similar to wild-type enzyme
S239A
activity is similar to wild-type enzyme
S239C
impaired activity possibly caused by disulfide mispairing
T58M
mutation in a late-onset case of recurrent acute pancreatitis. The T58M mutant chymotrypsin C has comparable biochemical characteristics to wild type enzyme on large substrates
V250E
natural missense variant, 0.08% of wild-type activity
additional information
-
deletion mutant K247_R254del shows diminished activity
A73T
-
diminished activity
A73T
natural missense variant, 62% of wild-type activity
G217S
-
specific activity is about 7% of the wild type enzyme
G217S
natural missense variant, 0.5% of wild-type activity
Q48R
-
mutant shows about 30% activity of the wild type enzyme
Q48R
natural missense variant, 85% of wild-type activity
R254W
-
shows about 50% of wild-type activity
R254W
natural missense variant, 100% of wild-type activity
R37Q
-
mutant shows essentially normal activity and secretion (about 82-88% activity of the wild type enzyme)
R37Q
natural missense variant, 64% of wild-type activity
V235I
-
CTRC activity secreted by cells transfected with variant V235I is moderately reduced (about 65% of the wild type enzyme)
V235I
natural missense variant, 73% of wild-type activity
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Developmental regulation of the porcine exocrine pancreas by glucocorticoids
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Electrophoretic separation of proteolytic enzymes in pancreatic juice collected with the pouch or catheter method
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281
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Mus musculus
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Indian J. Exp. Biol.
45
998-1002
2007
Conogethes punctiferalis
brenda
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40
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2008
Homo sapiens
brenda
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104
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2007
Homo sapiens (Q99895), Homo sapiens
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62
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288
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290
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