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Information on EC 3.4.21.1 - chymotrypsin and Organism(s) Bos taurus and UniProt Accession P00766

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.1 chymotrypsin
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Select one or more organisms in this record: ?
This record set is specific for:
Bos taurus
UNIPROT: P00766 not found.
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage: Tyr-/-, Trp-/-, Phe-/-, Leu-/-
Synonyms
chymotrypsin, alpha-chymotrypsin, bovine alpha-chymotrypsin, chymotrypsin a, alpha-ct, chymotrypsin b, chtp, alpha chymotrypsin, alpha-chymotrypsin a, chymotrypsin ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-Chy
-
alpha-chymotrypsin
chymotrypsin
-
4CHA
-
-
Alcalase
-
-
alpha chymar
-
-
-
-
alpha chymotrypsin
-
-
alpha-chymar ophth
-
-
-
-
alpha-chymotrypsin
alpha-chymotrypsin A
-
-
-
-
avazyme
-
-
-
-
bovine alpha-chymotrypsin
-
-
Chtp
-
-
ChTRP
-
-
chymar
-
-
-
-
chymotest
-
-
-
-
chymotrypsin A
-
-
-
-
chymotrypsin B
-
-
-
-
EC 3.4.4.6
-
-
-
-
enzeon
-
-
-
-
quimar
-
-
-
-
quimotrase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9004-07-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
?
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
show the reaction diagram
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
?
L-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine 4-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine-4-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosyl-ethyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-glutaryl-L-phenylalanine-4-nitroanilide + H2O
N-glutaryl-L-phenylalanine + 4-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
-
-
?
N-succinyl-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Gly-Gly-4-nitroanilide + H2O
N-succinyl-Gly-Gly + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-phenylalanine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
?
2-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]ethanaminium + H2O
?
show the reaction diagram
-
-
-
-
?
4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
4-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]butanoate + 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
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
?
benzoyl-4-guanidinophenyl ester + H2O
benzoyl + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-D-Ala-4-guanidinophenyl ester + H2O
benzoyl-D-Ala + 4-guanidinophenol
show the reaction diagram
-
5% of activity with N-benzoyl-L-Ala-4-guanidinophenyl ester
-
?
benzoyl-D-Leu-4-guanidinophenyl ester + H2O
benzoyl-D-Leu + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-D-Phe-4-guanidinophenyl ester + H2O
benzoyl-D-Phe + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-Gly-4-guanidinophenyl ester + H2O
benzoyl-Gly + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-L-Ala-4-guanidinophenyl ester + H2O
benzoyl-L-Ala + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-L-tyrosine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Tyr-p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-tyrosine p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
beta-lactoglobulin A + H2O
?
show the reaction diagram
-
-
chymotrypsin hydrolyzes beta-lactoglobulin A after Tyr, Trp, Phe, Met, and Leu, peptides corresponding to the cleavage of bonds with Glu, Gln, and Lys at the N-terminal side are also found
-
?
bovine chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
bovine serum albumine + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
cheese whey protein + H2O
?
show the reaction diagram
-
-
-
-
r
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
1 mM in 25mM Tris-HCl buffer containing 0.5M NaCl
-
-
?
L-Tyr ethyl ester + H2O
L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
m-calpain + H2O
fragments of m-calpain
show the reaction diagram
-
-
-
?
mu-calpain + H2O
fragments of mu-calpain
show the reaction diagram
-
-
-
?
N-acetyl-DL-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-DL-Phe-beta-naphthylester + H2O
N-acetyl-DL-Phe + beta-naphthol
show the reaction diagram
-
-
-
?
N-acetyl-DL-phenylglycine methyl ester + H2O
N-acetyl-L-phenylglycine + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-L-leucine methyl ester + H2O
N-acetyl-L-leucine + methanol
show the reaction diagram
-
5% of kcat with N-acetyl-L-tyrosine ethyl ester
-
?
N-acetyl-L-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
-
?
N-acetyl-L-Phe-Ala-Thr-Pal-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Pal + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOH)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOH) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Tyr + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + glycinamide
N-Ac-Phe-Gly-NH2 + ethanol
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + H2O
N-acetyl-L-phenylalanine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-tryptophan ethyl ester + H2O
N-acetyl-L-tryptophan + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr-ethyl ester + H2O
N-acetyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr-p-nitroanilide + H2O
N-acetyl-L-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
N-alpha-acetyl-L-tyrosine ethyl ester + H2O
N-alpha-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
? + p-nitroaniline
show the reaction diagram
-
BApNA
-
-
?
N-alpha-benzoyl-L-tyrosine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-tyrosyl ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-arginine ethyl ester + H2O
N-benzoyl-L-arginine + ethanol
show the reaction diagram
-
0.5 mM in 50 mM phosphate buffer, pH 7.6
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
N-benzoyl-L-Tyr-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
N-benzoyl-L-tyrosine ethyl ester + methanol
N-benzoyl-L-tyrosine methyl ester + ethanol
show the reaction diagram
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + ethanol
N-benzoyl-L-tyrosine ethyl ester + methanol
show the reaction diagram
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + H2O
N-benzoyl-L-tyrosine + methanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-Tyr p-nitroanilide + H2O
N-benzoyl-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid + H2O
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid + H2O
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-glutamyl-L-phenylalanine p-nitroanilide + H2O
p-nitroaniline + N-glutamyl-L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-glutaryl-L-Phe-p-nitroanilide + H2O
N-glutaryl-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-glutaryl-L-phenylalanine-p-nitroanilide + H2O
N-glutaryl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Ala p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Arg + p-nitroaniline
show the reaction diagram
-
very low activity
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Lys + p-nitroaniline
show the reaction diagram
-
extremly low activity
-
?
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nle + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nva + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-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 + 4-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
N-succinyl-Ala-Phe-Ala + H2O
N-succinyl-Ala-Phe + alanine
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
show the reaction diagram
N-succinyl-L-phenylalanine p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Phe-p-nitroanilide + H2O
p-nitroaniline + N-succinyl-Phe
show the reaction diagram
-
-
-
-
?
N-[1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]-N'-[2-[2-(2-hydroxyethoxy)ethoxy]ethyl]butanediamide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Ala + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Leu p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Leu + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Tyr + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-L-Tyr benzyl ester + H2O
Nalpha-tosyl-L-Tyr + phenol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
succinimidyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinimidyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-Thr-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Z-Phe-Arg-Thr-Tyr + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bovine chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
required for catalysis
Cd2+
CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations
Ca2+
-
5 mM, 1.5fold increase in activity, destabilizes the enzyme-pancreatic trypsin inhibitor complex formation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-propanediol
residual activity of bovine pancreatic alpha-chymotrypsin is studied in water/1,2-propanediol mixtures in the entire range of water content at 25°C. The degree of stabilization/ destabilization of alpha-chymotrypsin depends strongly on the water content in organic solvent. At high water content, the residual activity values are higher than 100%. At low water content, the residual catalytic activity is about 90-95%, compared with that observed after incubation in pure water
2-(2,6-difluorophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(2,6-dimethoxyphenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
2-(2-bromophenyl)-4H-3,1-benzoxazin-4-one
competitive inhibition
2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
2-(2-methoxyphenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(2-methylphenyl)-4H-3,1-benzoxazin-4-one
competitive inhibition
2-(2-nitrophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(2-thienyl)-4H-3,1-benzoxazin-4-one
competitive inhibition
2-(3,4,5-trimethoxyphenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(3-bromophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(3-bromophenyl)-7-nitro-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(3-chlorophenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
2-(3-chlorophenyl)-7-methyl-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(3-fluorophenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
2-(3-methylphenyl)-4H-3,1-benzoxazin-4-one
competitive inhibition
2-(3-methylphenyl)-7-nitro-4H-3,1-benzoxazin-4-one
competitive inhibition
2-(3-nitrophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(4-bromophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(4-fluorophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(4-methoxyphenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-(4-methylphenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
2-(4-nitrophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
2-oxo-2-(1,2,7,8-tetradehydro-5,6-dihydro-4-benzazecin-4(3H)-yl)ethyl N-(tert-butoxycarbonyl)-L-phenylalaninate
enediyne-amino acid conjugate, competitive inhibitor
2-oxo-2-(piperidin-1-yl)ethyl N-(tert-butoxycarbonyl)-L-phenylalaninate
piperidine amino acid conjugate, exhibits lesser inhibitory activity compared to the enediyne-peptide conjugates
2-oxo-2-[(5Z)-3,4,7,8-tetradehydro-9,10-dihydroazecin-1(2H)-yl]ethyl N-(tert-butoxycarbonyl)-L-phenylalaninate
enediyne-amino acid conjugate
2-phenyl-4H-3,1-benzoxazin-4-one
mixed-type inhibition
4-methyl-N-[2-(4-oxo-4H-3,1-benzoxazin-2-yl)phenyl]benzenesulfonamide
non-competitive inhibition
4-[(4-nitrophenyl)sulfonyl]-1,2,7,8-tetradehydro-3,4,5,6-tetrahydro-4-benzazecine
-
7-chloro-2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
mixed-type inhibition
7-chloro-2-(2-methylphenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
7-chloro-2-(4-nitrophenyl)-4H-3,1-benzoxazin-4-one
non-competitive inhibition
7-chloro-2-phenyl-4H-3,1-benzoxazin-4-one
non-competitive inhibition
7-hydroxycoumarin
0.78 mM, 50% inhibition
benzoxazinone
the presence of substituents on benzene ring reduces the inhibitory potential of benzoxazinone. The increased inhibitory potential due to fluoro group at phenyl substituent is observed followed by chloro and bromo substituents. Compounds with strong electron donating or withdrawing groups on phenyl substituent, show a good inhibitory potential at ortho > meta > para position. Kinetic studies show diverse types of inhibition, except uncompetitive-type inhibition
black-eyed pea trypsin/chymotrypsin inhibitor
BTCI, is able to inhibit trypsin and chymotrypsin simultaneously by forming a stable ternary complex
-
chymostatin
competitive inhibition
complex of vanadate and benzohydroxamic acid
competitive inhibitor of alpha-chymotrypsin, consisting of 1 mM vanadate and 2 mM benzohydroxamic acid
cyanopeptolin
Arg-containing cyanopeptolins inhibit trypsin at low IC50 values (0.00024-0.00026 mM)and show mild activity against chymotrypsin (IC50 0.0031-0.0038 mM), while Tyr-containing cyanopeptolins are selectively and potently active against chymotrypsin (IC50 0.00026 mM). Neither of the cyanopeptolins are active against thrombin, elastase or protein phosphatase 1. Two cyanopeptolins (CP962 and CP985) have no cytotoxic effects on MCF-7 breast cancer cells. Strong and selective activity of the new cyanopeptolin variants makes them potential candidates for the development of drugs against metabolic disorders and other diseases
-
cyanopeptolin 1020
isolated from Nostoc edaphicum CCNP1411
cyanopeptolin 1027
isolated from Nostoc edaphicum CCNP1411
cyanopeptolin 978
isolated from Nostoc edaphicum CCNP1411
cyanopeptolin 985
isolated from Nostoc edaphicum CCNP1411
cyanopeptolin 992
isolated from Nostoc edaphicum CCNP1411
N-(2-acetylphenyl)-N'-(3-methylphenyl) urea
-
N-(2-methylphenyl)-2-oxo-1-pyrrolidine carboxamide
most active inhibitor
N-(tert-butoxycarbonyl)-L-alanyl-N-[4-[2-(3-oxoprop-1-yn-1-yl)phenyl]but-3-yn-1-yl]-L-phenylalaninamide
enediyne-amino acid conjugate
Proflavin
-
tert-butyl [(2S)-1-(3,4-dihydroquinolin-1(2H)-yl)-1-oxo-3-phenylpropan-2-yl]carbamate
isoquinoline amino acid conjugate, exhibits lesser inhibitory activity compared to the enediyne-peptide conjugates, does not interact directly with the catalytic triad of chymotrypsin
tert-butyl [(2S)-1-oxo-3-phenyl-1-(1,2,7,8-tetradehydro-5,6-dihydro-4-benzazecin-4(3H)-yl)propan-2-yl]carbamate
enediyne-amino acid conjugate
(Cbz-alanyl)aminomethyl boronic acid
-
inhibition decreases in the presence of arabinogalactan
(Cbz-phenylalanyl)aminomethyl boronic acid
-
inhibition decreases in the presence of arabinogalctan
(S)-(1-benzyl-2-thiolethyl)-carbamic acid benzyl ester
-
inhibition of alpha-chymotrypsin in the presence of Zn2+
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
2,2'-[[(1-[[1-(tert-butoxycarbonyl)-L-prolyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-3,1-diyl)]diacetic acid
-
-
2,3-dichlorophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
2,5-dichlorophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
2-hydroxymethyl-1-(2-phenylethanecarbonyl)pyrrole
-
0.0125 mg/ml, 10% inhibition
2-hydroxymethyl-1-(2-phenylethansulfonyl)pyrrole
-
0.0125 mg/ml, 15% inhibition
2-hydroxymethyl-1-(2-phenylethenylsulfonyl)pyrrole
-
0.0125 mg/ml, 15% inhibition
2-hydroxymethyl-1-(N-phthalyl-L-leucine)pyrrole
-
0.0125 mg/ml, 10% inhibition
2-hydroxymethyl-1-(phenylsulfonyl)pyrrole
-
0.053 mM, 20% inhibition
2-nitrophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3,5-dichlorophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-bromophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-chloro-5-methoxyphenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-chlorophenyl-6(acetoxymethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-chlorophenyl-6-methyl-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-fluorophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-methoxyphenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
3-trifluoromethylphenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
4-fluorophenylboronic acid
-
-
Ac-Phe-Val-Thr-p-amino-L-phenylalanine-CHO
-
-
Ac-Phe-Val-Thr-p-nitro-L-phenylalanine-CHO
-
-
Ac-Phe-Val-Thr-Phe-CHO
-
-
Ac-Phe-Val-Thr-pyridyl-L-alanine-CHO
-
-
Ac-Phe-Val-Thr-Tyr-CHO
-
-
Acacia plumosa trypsin inhibitor A
-
strong inhibition
-
Acacia plumosa trypsin inhibitor B
-
strong inhibition
-
Acacia plumosa trypsin inhibitor C
-
strong inhibition
-
alpha1-Aantichymotrypsin
-
forms very long-lived, enzymatically inactive 1/1 compexes with its target
-
alpha2-Macroglobulin
-
nonspecific proteinase inhibitor
-
Alzheimer's amyloid beta-protein precursor
-
engineering of inhibitors with altered specificities
-
anti-trypsin-chymotrypsin A
-
highly potent serine protease inhibitor protein from Theromyzon tessulatum
-
anti-trypsin-chymotrypsin B
-
highly potent serine protease inhibitor protein from Theromyzon tessulatum
-
Aprotinin
-
-
AVPGSWPW
-
octapeptide
basic pancreatic trypsin inhibitor
-
benzamidine
-
-
benzyloxycarbonyl-Ala-Ala-Phe-glyoxal
-
-
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
benzyloxycarbonyl-Phe-glyoxal
-
-
benzyloxycarbonyl-Pro-Phe-glyoxal
-
-
BGTI1
-
concentration 228 nM: 100% inhibition, concentration 456 nM: 97.8% inhibition, concentration 114 nM: 73.3% inhibition, concentration 57 nM: 41.3% inhibition. Inhibitor from Vigna mungo seeds
-
BGTI2
-
concentration 2188 nM: 53.3% inhibition, concentration 1094 nM: 28.9% inhibition, concentration 547 nM: 11.1% inhibition, concentration 273 nM: 6.7% inhibition. Inhibitor from Vigna mungo seeds
-
BGTI3
-
concentration 5000 nM: 36.7% inhibition, concentration 2500 nM: 22.3% inhibition, concentration 1250 nM: 10.0% inhibition, concentration 625 nM: 0.0% inhibition. Inhibitor from Vigna mungo seeds
-
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
one of the most potent inhibitors of chymotrypsin within phosphonic analogs of phenylalanine
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bovine basic panreatic trypsin inhibitor
-
-
-
Bovine pancreatic trypsin inhibitor
-
300fold stronger inhibition of alpha-chymotrypsin in the presence of 3 M NaCl
-
Bowman-Birk inhibitor
-
-
brein 3-O-myristate
-
0.000078 mM, 50% inhibition, noncompetitive inhibition
brein 3-O-palmitate
-
0.000042 mM, 50% inhibition, noncompetitive inhibition
broad bean trypsin-chymotrypsin inhibitor
-
7500 Da peptide isolated from from Vicia faba, almost complete inhibition at a molar ratio of 20
-
chymostatin
-
-
cycloart-24-ene-3beta-ol
-
0.00014 mM, 50% inhibition, noncompetitive inhibition
cyclododecyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
cyclohexyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
cyclo[-Gly-Arg-cyclo[-S-Cys-Thr-Lys-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp-]
-
sunflower trypsin inhibitor, SFTI-1
dammara-20,24-dien-3beta-ol
-
0.00013 mM, 50% inhibition, competitive inhibition
diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
Eglin c
-
-
faradiol 3-O-myristate
-
0.000032 mM, 50% inhibition, noncompetitive inhibition
faradiol 3-O-palmitate
-
0.000072 mM, 50% inhibition, noncompetitive inhibition
GAW
-
tripeptide
Gly-Arg-cyclo[-S-Cys-Thr-Pal-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-CH3)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-F)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-guanidine)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-NH2)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-NO2)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Tyr-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
IVNGEEAVPGSWPW
-
autocatalytically produced 14-residue fragment from a three-phase-partitioning-treated chymotrypsin
Leu-Phe-p-fluorophenylmethylamide
-
strong inhibition
lima bean inhibitor
-
-
-
Lima bean trypsin inhibitor
-
-
-
lup-20(29)-ene-3beta,16beta-diol
-
0.00012 mM, 50% inhibition, competitive inhibition
maniladiol 3-O-myristate
-
0.000078 mM, 50% inhibition, competitive inhibition
maniladiol 3-O-palmitate
-
0.000084 mM, 50% inhibition, noncompetitive inhibition
methyl-4-hydroxy-4-[1-(phenylsulfonyl)pyrrol-2-yl]butanoate
-
0.0125 mg/ml, 10% inhibition
mixed monolayer protected gold cluster
-
anionically functionalized amphiphilic nanoparticles
-
N-(tert-butoxycarbonyl)-L-valyl-N-(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)-L-prolinamide
-
tripeptide containing leucine-related phosphonates, which is a relatively weak chymotrypsin inhibitor
N-(tert-butoxycarbonyl)-L-valyl-N-[1-(diphenoxyphosphoryl)-2-phenylethyl]-L-prolinamide
-
tripeptide containing leucine-related phosphonates, which is a relatively weak chymotrypsin inhibitor
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
tripeptide containing leucine-related phosphonates, which is a relatively weak chymotrypsin inhibitor
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
tripeptide containing leucine-related phosphonates, which is a relatively weak chymotrypsin inhibitor
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-tert-butylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
tripeptide containing leucine-related phosphonates, which is a relatively weak chymotrypsin inhibitor
N-acetyl-L-Phe-Ala-Thr-Pal aldehyde
-
-
N-acetyl-L-Phe-Ala-Thr-Phe aldehyde
-
-
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2) aldehyde
-
-
N-acetyl-L-Phe-Ala-Thr-Tyr aldehyde
-
-
N-alpha-tosyl-L-Phe chloromethyl ketone
-
TPCK
N-carbobenzoxy-Gly-Gly-Phe-chloromethyl ketone
-
Z-GGF-CK
N-succinyl-L-phenylalanine
-
-
N-toluenesulfonyl-L-phenylalanine chloromethyl-ketone
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, partially inhibits (53% residual activity)
N-tosyl-L-Phe-Ala-Thr-Phe-(p-NO2) aldehyde
-
-
p-octyloxybenzyltributylammonium bromide
-
5 mM, approx. 90% inactivation after 24 h
p-octyloxybenzyltrimethylammonium bromide
-
10 mM, complete inactivation
P1 bovine chymotrypsin-bovine pancreatic trypsin inhibitor
-
P1 BPTI, P1-Xaa variants
-
pars intercerebralis major peptide
-
i.e. PMP-C, potent alpha-chymotrypsin inhibitor protein from the insect Locusta migratoria
-
phenylboronic acid
-
-
phenylmethylsulfonyl-fluoride
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits (4% residual activity)
Phenylmethylsulfonylfluoride
-
the enzymatic activity is completely lost at 1 mM and room temperature
photolytic 1-(2-nitrophenyl)ethanol residues
-
1-(2-nitrophenyl)ethanol coated protein can be reactivated by 15 min UV-A radiation
-
Proflavin
-
substrate mimic inhibitor
S-(3'-chlorophenyl)-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carbothioate
-
-
Soybean trypsin inhibitor
-
Suc-Val-Pro-PheP(OPh)2
-
most potent phosphonate chymotrypsin inhibitor
taraxast-20(39)-ene-3beta,16beta-diol
-
0.000096 mM, 50% inhibition, noncompetitive inhibition
taraxast-20-ene-3beta,16beta-diol
-
0.00016 mM, 50% inhibition, competitive inhibition
tert-butyl (2S)-2-([1-[bis(2-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(3,4-dimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(4-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)carbamoyl]pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[[1-(diphenoxyphosphoryl)-2-phenylethyl]carbamoyl]pyrrolidine-1-carboxylate
-
-
tirucalla-7,24-dien-3beta-ol
-
0.000098 mM, 50% inhibition, noncompetitive inhibition
TPGVY
-
pentapeptide
trypsin-inhibitor
-
from Glycine max cv. Small Glossy Black
-
urs-12-ene-3beta,16beta-diol
-
0.00012 mM, 50% inhibition, noncompetitive inhibition
WCI2
-
Psophocarpus tetragonolobus chymotrypsin inhibitor retards growth of Helicoverpa armigera and strongly inhibits commercially available bovine chymotrypsin
-
WCI5
-
Psophocarpus tetragonolobus chymotrypsin inhibitor retards growth of Helicoverpa armigera and strongly inhibits commercially available bovine chymotrypsin
-
wheat subtilisin/chymotrypsin inhibitor
-
as the wild-type inhibitor, the recombinant inhibitor, while acting as a strong subtilisin inhibitor, is much less efficient against alpha-chymotrypsin. Mutant E49S of the wheat subtilisin/chymotrypsin inhibitor shows a limited anti-chymotrypsin activity. Mutants E49P, Y50G and M48P/E49G are inactive against alpha-chymotrypsin
-
winged bean chymotrypsin-trypsin inhibitor
-
inhibitor from Psophocarpus tetragonolobus, inhibits and binds trypsin and chymotrypsin in a 1:1 molar ratio. Complete inhibition of chymotrypsin with purified recombinant inhibitor at a 1:1 molar ratio, similarly to the inhibitor obtained from winged bean seeds
-
WSCI
-
proteinase inhibitor isolated from Triticum aestivum
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-propanediol
residual activity of bovine pancreatic alpha-chymotrypsin is studied in water/1,2-propanediol mixtures in the entire range of water content at 25°C. The degree of stabilization/ destabilization of alpha-chymotrypsin depends strongly on the water content in organic solvent. At high water content, the residual activity values are higher than 100%. At low water content, the residual catalytic activity is about 90-95%, compared with that observed after incubation in pure water
1,8-bis(tributylammonium)octane dibromide
provokes superactivation and stabilization effects in a way similar to cetyltributytetrabutylammonium bromide, but at lower concentration
benzyldodecyldimethylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
benzyltributylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
benzyltrimethylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
cetyltributylammonium bromide
provokes a superactivation of alpha-chymotrypsin in aqueous solution
dodecyltrimethylammonium bromide
in comparison to buffer the catalytic activity of the enzyme is enhanced 5fold in premicellar dodecyltrimethylammonium bromide solutions. Negligible changes are observed in cetyltrimethylammonium bromide and octadecyltrimethylammonium bromide
selenium nanoparticles
immobilization of the enzyme on selenium nanoparticles increases the proteolytic activity of the enzyme, making it possible to efficiently operate at suboptimal pH values (in an alkaline medium)
-
silica
the activity of alpha-chymotrypsin is enhanced upon adsorption on silica particles. Pressure increases the activity of adsorbed alpha-chymotrypsin further
-
spermine
-
tetrabutylammonium bromide
provokes a superactivation of alpha-chymotrypsin in aqueous solution
cetyltributylammonium bromide
-
promotes activity
dodecyltrimethylammonium bromide
-
2-20 mM
hexadecyltrimethylammonium bromide
-
2-60 mM, aqueous micelles of the cationic polymeric surfactant hexadecyltrimethylammonium bromide
p-octyloxybenzyltributylammonium bromide
-
maximal activation at 5 mM, inhibition at extended incubation
tetrabutylammonium bromide
tetrapentylammonium bromide
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 1.4
4-nitrophenyl acetate
0.032 - 0.098
4-nitrophenyl benzoate
0.59 - 1.1
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.01 - 0.18
N-benzoyl-L-tyrosine 4-nitroanilide
1.17 - 8.1
N-benzoyl-L-tyrosine ethyl ester
0.05 - 0.083
N-benzoyl-L-tyrosine-4-nitroanilide
0.067
N-benzoyl-L-tyrosyl-ethyl ester
pH 8.0, 37°C
0.44
N-glutaryl-L-phenylalanine-4-nitroanilide
pH 7.75, 25°C
0.024 - 0.375
N-succinyl-L-phenylalanine-4-nitroanilide
7.27
acetyl-L-Leu methyl ester
-
-
0.17
acetyl-L-Trp ethyl ester
-
-
1.04
acetyl-Phe ethyl ester
-
-
1.27
Acetyl-Tyr ethyl ester
-
-
1.05 - 6.79
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.44
benzoyl-4-guanidinophenyl ester
-
25°C, pH 7.6
4.94
benzoyl-D-Ala-4-guanidinophenyl ester
-
25°C, pH 7.6
1.49
benzoyl-D-Leu-4-guanidinophenyl ester
-
25°C, pH 7.6
2.58
benzoyl-D-Phe-4-guanidinophenyl ester
-
25°C, pH 7.6
2.81
benzoyl-Gly-4-guanidinophenyl ester
-
25°C, pH 7.6
2.88
benzoyl-L-Ala-4-guanidinophenyl ester
-
25°C, pH 7.6
0.13
benzoyl-Tyr ethyl ester
-
-
7.02
N-acetyl-L-leucine methyl ester
-
25°C, pH 7.5
0.0891
N-acetyl-L-Phe-Ala-Thr-Pal-5-amido-2-nitrobenzoic acid
-
-
0.0101
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN)-5-amido-2-nitrobenzoic acid
-
-
0.1131
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe)-5-amido-2-nitrobenzoic acid
-
-
0.1203
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine)-5-amido-2-nitrobenzoic acid
-
-
0.0635
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2)-5-amido-2-nitrobenzoic acid
-
-
0.001
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid
-
-
0.0191
N-acetyl-L-Phe-Ala-Thr-Phe-5-amido-2-nitrobenzoic acid
-
-
0.0598
N-acetyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid
-
-
1.12
N-acetyl-L-phenylalanine ethyl ester
-
25°C, pH 7.5
0.19
N-acetyl-L-tryptophan ethyl ester
-
25°C, pH 7.5
1.17
N-acetyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
0.939
N-alpha-benzoyl-DL-arginine-p-nitroanilide
-
-
0.24 - 0.27
N-benzoyl-L-Tyr ethyl ester
0.12 - 6.02
N-benzoyl-L-tyrosine ethyl ester
2.23 - 20.6
N-benzoyl-L-tyrosine methyl ester
0.11 - 0.21
N-benzoyl-Tyr p-nitroanilide
0.0009
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid
-
-
0.0177
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid
-
-
0.32 - 6.1
N-glutaryl-L-Phe-p-nitroanilide
0.013
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
0.32 - 3
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
0.26 - 0.44
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
0.32 - 2.6
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
0.02 - 0.37
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
0.052 - 0.58
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
0.16 - 1.6
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
0.05 - 0.19
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.0074 - 0.5
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
0.4 - 0.48
N-succinyl-Ala-Phe-Ala
2.5
N-succinyl-Ala-Phe-p-nitroanilide
-
30°C, pH 8.0
0.044
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide
-
at 25°C
0.14
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 25°C
1.09
N-succinyl-L-Phe-p-nitroanilide
-
at 25°C
0.022
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
-
3
N-succinyl-Phe-7-amido-4-methylcoumarin
-
-
0.09 - 0.1
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
0.62 - 0.64
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
0.08
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester
-
-
0.4
Nalpha-tosyl-L-Tyr benzyl ester
-
-
0.0297 - 0.044
p-nitrophenyl acetate
0.07
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.09
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30°C
0.8
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37°C
additional information
casein
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.1
4-nitrophenyl acetate
0.0075 - 0.047
4-nitrophenyl benzoate
0.45 - 0.6
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.013 - 2.3
N-benzoyl-L-tyrosine 4-nitroanilide
0.04 - 0.5
N-benzoyl-L-tyrosine-4-nitroanilide
0.00942
N-benzoyl-L-tyrosyl-ethyl ester
pH 8.0, 37°C
0.0146
N-glutaryl-L-phenylalanine-4-nitroanilide
pH 7.75, 25°C
0.154 - 1.177
N-succinyl-L-phenylalanine-4-nitroanilide
6.6
acetyl-L-Leu methyl ester
-
-
48.4
acetyl-L-Trp ethyl ester
-
-
52.4
acetyl-Phe ethyl ester
-
-
126
Acetyl-Tyr ethyl ester
-
-
0.66 - 21.7
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.13
benzoyl-4-guanidinophenyl ester
-
25°C, pH 7.6
0.56 - 6.08
benzoyl-D-Ala-4-guanidinophenyl ester
3 - 6
benzoyl-D-Leu-4-guanidinophenyl ester
5.54
benzoyl-D-Phe-4-guanidinophenyl ester
-
25°C, pH 7.6
1.18 - 6.08
benzoyl-Gly-4-guanidinophenyl ester
10.4
benzoyl-L-Ala-4-guanidinophenyl ester
-
25°C, pH 7.6
76.6
benzoyl-Tyr ethyl ester
-
-
6.5
N-acetyl-L-leucine methyl ester
-
25°C, pH 7.5
6.4
N-acetyl-L-Phe-Ala-Thr-Pal-5-amido-2-nitrobenzoic acid
-
-
3
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN)-5-amido-2-nitrobenzoic acid
-
-
0.3
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe)-5-amido-2-nitrobenzoic acid
-
-
6.5
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine)-5-amido-2-nitrobenzoic acid
-
-
16.2
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2)-5-amido-2-nitrobenzoic acid
-
-
0.6
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid
-
-
6.1
N-acetyl-L-Phe-Ala-Thr-Phe-5-amido-2-nitrobenzoic acid
-
-
22.7
N-acetyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid
-
-
54.8
N-acetyl-L-phenylalanine ethyl ester
-
25°C, pH 7.5
48.8
N-acetyl-L-tryptophan ethyl ester
-
25°C, pH 7.5
130 - 220
N-acetyl-L-Tyr-ethyl ester
0.1 - 0.19
N-acetyl-L-Tyr-p-nitroanilide
119.5 - 120
N-acetyl-L-tyrosine ethyl ester
0.611
N-alpha-benzoyl-DL-arginine-p-nitroanilide
-
-
43 - 142
N-benzoyl-L-Tyr ethyl ester
0.03 - 70.4
N-benzoyl-L-tyrosine ethyl ester
2.34 - 10.8
N-benzoyl-L-tyrosine methyl ester
0.05 - 0.41
N-benzoyl-Tyr p-nitroanilide
1.8
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid
-
-
16.7
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid
-
-
0.015 - 0.31
N-glutaryl-L-Phe-p-nitroanilide
0.014 - 0.05
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
0.031 - 16
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
0.006 - 0.34
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
1.45 - 15
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
12 - 18
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
0.04 - 9.31
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
6.2 - 13.5
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
77 - 110
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
0.9 - 1.2
N-succinyl-Ala-Phe-Ala
0.65
N-succinyl-Ala-Phe-p-nitroanilide
-
30°C, pH 8.0
39
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide
-
at 25°C
7.8
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 25°C
0.014
N-succinyl-L-Phe-p-nitroanilide
-
at 25°C
0.008 - 6.43
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
0.6
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
-
at pH 4.0
85
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester
-
-
21.4
Nalpha-tosyl-L-Tyr benzyl ester
-
-
0.017 - 0.028
p-nitrophenyl acetate
1.9
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30°C
0.9
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37°C
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.144
4-nitrophenyl acetate
0.141 - 0.668
4-nitrophenyl benzoate
0.23 - 220
N-benzoyl-L-tyrosine 4-nitroanilide
0.48 - 10
N-benzoyl-L-tyrosine-4-nitroanilide
0.14
N-benzoyl-L-tyrosyl-ethyl ester
pH 8.0, 37°C
0.0332
N-glutaryl-L-phenylalanine-4-nitroanilide
pH 7.75, 25°C
2.74 - 6.47
N-succinyl-L-phenylalanine-4-nitroanilide
21
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30°C
1100
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0301
2-(2,6-difluorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0277
2-(2,6-dimethoxyphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0091
2-(2-bromophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.00047
2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0125
2-(2-methoxyphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0098
2-(2-methylphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0224
2-(2-nitrophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0091
2-(2-thienyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0226
2-(3-chlorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0178
2-(3-fluorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0161
2-(3-methylphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.01619
2-(3-methylphenyl)-7-nitro-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.341
2-(3-nitrophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.094
2-(4-fluorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0126
2-(4-methoxyphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0164
2-(4-methylphenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.03
2-oxo-2-(1,2,7,8-tetradehydro-5,6-dihydro-4-benzazecin-4(3H)-yl)ethyl N-(tert-butoxycarbonyl)-L-phenylalaninate
in 80 mM Tris HCl buffer, pH 7.8 and 3 M CaCl2
0.75
2-oxo-2-(piperidin-1-yl)ethyl N-(tert-butoxycarbonyl)-L-phenylalaninate
in 80 mM Tris HCl buffer, pH 7.8 and 3 M CaCl2
0.0087
2-phenyl-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.303
7-chloro-2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
pH 7.6, 30°C
0.0026
chymostatin
pH 7.6, 30°C
0.014
complex of vanadate and benzohydroxamic acid
in 20 mM sodium cacodylate (pH 7.4) and 75% saturated ammonium sulfate
0.012
N-(tert-butoxycarbonyl)-L-alanyl-N-[4-[2-(3-oxoprop-1-yn-1-yl)phenyl]but-3-yn-1-yl]-L-phenylalaninamide
in 80 mM Tris HCl buffer, pH 7.8 and 3 M CaCl2
0.003
tert-butyl [(2S)-1-oxo-3-phenyl-1-(1,2,7,8-tetradehydro-5,6-dihydro-4-benzazecin-4(3H)-yl)propan-2-yl]carbamate
in 80 mM Tris HCl buffer, pH 7.8 and 3 M CaCl2
1.08
(Cbz-alanyl)aminomethyl boronic acid
-
37°C, pH 8.0
1.96
(Cbz-phenylalanyl)aminomethyl boronic acid
-
37°C, pH 8.0
0.00001
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0027
2,2'-[[(1-[[1-(tert-butoxycarbonyl)-L-prolyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-3,1-diyl)]diacetic acid
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
31.01
4-fluorophenylboronic acid
-
37°C, pH 8.0
0.00057
Ac-Phe-Val-Thr-p-amino-L-phenylalanine-CHO
-
-
0.0000032
Ac-Phe-Val-Thr-p-nitro-L-phenylalanine-CHO
-
-
0.000011
Ac-Phe-Val-Thr-Phe-CHO
-
-
0.001
Ac-Phe-Val-Thr-pyridyl-L-alanine-CHO
-
-
0.0000017
Ac-Phe-Val-Thr-Tyr-CHO
-
-
0.00001
Acacia plumosa trypsin inhibitor A
-
in phosphate buffer saline, pH 7.4, at 37°C for 30 min
-
0.0000102
Acacia plumosa trypsin inhibitor B
-
in phosphate buffer saline, pH 7.4, at 37°C for 30 min
-
0.0000109
Acacia plumosa trypsin inhibitor C
-
in phosphate buffer saline, pH 7.4, at 37°C for 30 min
-
0.00000000035
anti-trypsin-chymotrypsin A
-
-
-
0.0000000004
anti-trypsin-chymotrypsin B
-
-
-
0.000018
Aprotinin
-
25°C, pH 7.5
0.00000099
AVPGSWPW
-
-
0.344
benzyloxycarbonyl-Ala-Ala-Phe-glyoxal
-
at 25°C
0.000025 - 0.024
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
0.065
benzyloxycarbonyl-Phe-glyoxal
-
-
0.00085
benzyloxycarbonyl-Pro-Phe-glyoxal
-
37°, pH 7.4
0.00002
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.02
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.015
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0062
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00014
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0015
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.000045
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0013
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0033
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00065
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.11
brein 3-O-myristate
-
-
0.11
brein 3-O-palmitate
-
-
0.42
cycloart-24-ene-3beta-ol
-
-
0.06
dammara-20,24-dien-3beta-ol
-
-
0.0047
diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.03
faradiol 3-O-myristate
-
-
0.058
faradiol 3-O-palmitate
-
-
0.0047
GAW
-
-
0.000000027
IVNGEEAVPGSWPW
-
-
0.00017
Lima bean trypsin inhibitor
-
25°C, pH 7.5
-
0.057
lup-20(29)-ene-3beta,16beta-diol
-
-
0.026
maniladiol 3-O-myristate
-
-
0.12
maniladiol 3-O-palmitate
-
-
0.00001
mixed monolayer protected gold cluster
-
-
-
0.00005
N-(tert-butoxycarbonyl)-L-valyl-N-(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)-L-prolinamide
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00036
N-(tert-butoxycarbonyl)-L-valyl-N-[1-(diphenoxyphosphoryl)-2-phenylethyl]-L-prolinamide
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00033
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00179
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.00075
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-tert-butylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.003432
N-acetyl-L-Phe-Ala-Thr-Pal aldehyde
-
in Tris-HCl buffer with 20 mM CaCl2, at pH 8.3
0.000323
N-acetyl-L-Phe-Ala-Thr-Phe aldehyde
-
in Tris-HCl buffer with 20 mM CaCl2, at pH 8.3
0.000159
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2) aldehyde
-
in Tris-HCl buffer with 20 mM CaCl2, at pH 8.3
0.000281
N-acetyl-L-Phe-Ala-Thr-Tyr aldehyde
-
in Tris-HCl buffer with 20 mM CaCl2, at pH 8.3
0.0000112
N-tosyl-L-Phe-Ala-Thr-Phe-(p-NO2) aldehyde
-
in Tris-HCl buffer with 20 mM CaCl2, at pH 8.3
9.7
phenylboronic acid
-
37°C, pH 8.0
0.0019
Soybean trypsin inhibitor
-
25°C, pH 7.5
-
0.000074
Suc-Val-Pro-PheP(OPh)2
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.063
taraxast-20(39)-ene-3beta,16beta-diol
-
-
0.068
taraxast-20-ene-3beta,16beta-diol
-
-
0.0005
tert-butyl (2S)-2-([1-[bis(2-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0046
tert-butyl (2S)-2-([1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0108
tert-butyl (2S)-2-([1-[bis(3,4-dimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.02
tert-butyl (2S)-2-([1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.02
tert-butyl (2S)-2-([1-[bis(4-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.073
tert-butyl (2S)-2-[(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)carbamoyl]pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.0104
tert-butyl (2S)-2-[[1-(diphenoxyphosphoryl)-2-phenylethyl]carbamoyl]pyrrolidine-1-carboxylate
-
in 100 mM HEPES buffer, 500 mM NaCl, pH 7.5, 9% dimethyl sulfoxide
0.072
tirucalla-7,24-dien-3beta-ol
-
-
0.000034
TPGVY
-
-
0.11
urs-12-ene-3beta,16beta-diol
-
-
0.00000188
winged bean chymotrypsin-trypsin inhibitor
-
Dixon plot analysis, same for recombinant inhibitor and inhibitor obtained from winged bean seeds
-
0.0000072
WSCI
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0235
2-(2,6-difluorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0263
2-(2,6-dimethoxyphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0188
2-(2-bromophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0065
2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0099
2-(2-methoxyphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0288
2-(2-methylphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0238
2-(2-nitrophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0121
2-(2-thienyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0418
2-(3-chlorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0282
2-(3-fluorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0239
2-(3-methylphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0941
2-(3-methylphenyl)-7-nitro-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.314
2-(3-nitrophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.159
2-(4-fluorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0144
2-(4-methoxyphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0201
2-(4-methylphenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0117
2-phenyl-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.329
7-chloro-2-(2-fluorophenyl)-4H-3,1-benzoxazin-4-one
Bos taurus
pH 7.6, 30°C
0.0058
chymostatin
Bos taurus
pH 7.6, 30°C
0.0031
cyanopeptolin 1020
Bos taurus
pH 7.5, 37°C
0.00026
cyanopeptolin 1027
Bos taurus
pH 7.5, 37°C
0.0038
cyanopeptolin 978
Bos taurus
pH 7.5, 37°C
0.00026
cyanopeptolin 985
Bos taurus
pH 7.5, 37°C
0.0035
cyanopeptolin 992
Bos taurus
pH 7.5, 37°C
0.0136
N-(2-acetylphenyl)-N'-(3-methylphenyl) urea
Bos taurus
pH 7.6, 25°C
0.00824
N-(2-methylphenyl)-2-oxo-1-pyrrolidine carboxamide
Bos taurus
pH 7.6, 25°C
0.0148
trypsin-inhibitor
Bos taurus
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0034
-
casein proteolysis
36
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, on the amide substrate
44.6
-
hydrolysis of N-alpha-acetyl-L-tyrosine ethyl ester
84
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, on the ester substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
when immobilized on on magnetic nanogels
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
low activity chymotrypsin I and II at acidic pH (4–5), considerably activity at pH from 6 to 9
6 - 9.3
-
pH 6.0: about 35% of maximal activity, pH 9.3: 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35.8
-
-
37
-
temperature-dependent efficiency of catalysis reveals a bell-shaped feature with a peak at 37°C
58
-
after modification of alpha-chymotrypsin with mono-6-formyl-beta-cyclodextrin and mono-6-succinyl-6-deoxy-beta-cyclodextrin
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 62
-
approx. 50% of maximal activity at 20°C, approx. 20% of maximal activity at 62°C
37 - 40
-
catalytic activity of the enzyme exponentially falls off after 40°C and is thought to be associated with the thermal denaturation of the protein, the kcat and KM values associated with the enzyme catalysis increase up to 40°C and then fall
5 - 45
-
-
55 - 70
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
-
isoelectric focusing
8.8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CTRA_BOVIN
245
0
25666
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
-
25210
-
MALDI-TOF analysis
additional information
-
43000, recombinant winged bean chymotrypsin-trypsin inhibitor in complex with chymotrypsin, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
-
chemical modification of the surface exposed lysine amino groups of alpha-CT with activated poly(ethylene glycol)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown from 52% ammonium sulfate as precipitant containing 10 mg/ml of gamma-chymotrypsin, 100 mM sodium-cacodylate, pH 7.0 and 2.5% dioxane using the hanging-drop vapor diffusion method, crystals of gamma-chymotrypsin complexed with 7-hydroxycoumarin diffract to 1.8 A
hanging drop vapour diffusion method in 10 mM sodium cacodylate pH 6.0, 0.75% saturated cetyltrimethylammonium bromide, 45% saturated ammonium sulfate, and 1 M NaI solution
in complex with the black-eyed pea trypsin/chymotrypsin inhibitor, by hanging drop vapour diffusion method with 0.1 M HEPES pH 7.5, 10% (w/v) polyethylene glycol 6000, and 5% (v/v) 2-methyl-2,4-pentanediol as precipitant
time-of-flight neutron diffraction data collected from gamma-chymotrypsin to 2.0 A resolution. The catalytic histidine is doubly deuterated. The serine and aspartate that make up the remainder of the catalytic triad do not show density corresponding to the presence of deuterium. There is also deuteration of backbone NH at terminal positions of beta-sheets
alpha-chymotrypsin/eglin c complex at 2.6 A resolution
-
alpha-chymotrypsin:Kunitz-inhibitor complex
-
chymotrypsin complexed to the inhibitors domain of Alzheimer's amyloid beta-protein precursor, APPI, and basic pancreatic trypsin inhibitor, engineering of inhibitors with altered specificities
-
crystals of chymotrypsin complexed with the inhibitor Leu-Phe-p-fluorophenylmethylamide
-
hanging drop vapour diffusion method
-
hanging-drop method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the entrapment of alpha-chymotrypsin within 70-40 nm liposomes formed from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine leads to a remarkable increase in the thermal stability of the enzyme. Heating aqueous suspensions of alpha-chymotrypsin-containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes to 80°C for 30 minutes results in partial enzyme inactivation, whereas the same treatment of aqueous solutions of free enzyme inactivates the enzyme completely. The stabilizing effect of enzyme confinement in the attoliter volumes of the liposomes increases with decreasing numbers of alpha-chymotrypsin molecules per liposome
25
-
retaining around 85% of the initial activity after 2 h
35 - 55
-
approx. 50% loss of activity after 10 min at 50°C, complete loss of activity after 10 min at 55°C
40
-
is inactivated at 60°C
49.5
-
melting temperature
52.8
-
melting temperature
75 - 85
-
almost no activity is retained when the incubation temperature is above 75°C, the activity of the nanogel-bound alpha-CT still has a residual activity of 88.7% at 85°C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1,8-bis(tributylammonium)octane dibromide provokes stabilization effects in a way similar to cetyltributytetrabutylammonium bromide, but at lower concentration
autolysis of alpha-chymotrypsin is impeded when the enzyme is adsorbed on silica particles
enzyme stability is analyzed in 0.05 M Tris-HCl buffer pH 8.20 in the presence or the absence of methylamine, urea or methylamine + urea mixture of various concentrations at 25°C for 4 h to attain complete equilibrium. Indication that methylamines suppress the aggregation of a thermal denatured protein and that methylamines have comparable effects on counteracting the temperature-perturbing actions on alpha-chymotrypsin.
immobilization of the enzyme on selenium nanoparticles increases the stability
stability of the enzyme is increased in the presence of spermine
the enzyme becomes more stable in the presence of L-Met, based on the molecular dynamics simulation
alpha-chymotrypsin immobilized on mesoporous silica is stable for at least 1 week, i.e. 20 recycles per day, at room temperature, activity decreases gradually to 15% during next 10 days
-
in the presence of putrescine and spermidine a clear stabilizing effect against thermal unfolding is achieved
-
lanthanide ions, e.g. terbium accelerates the inactivation process
-
protects the enzyme from inactivation process, probably of autolytic nature
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulfoxide
study on the influence of different water-dimethyl sulfoxide mixtures encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles on the enzymatic hydrolysis of N-benzoyl-L-tyrosine p-nitroanilide by alpha-chymotrypsin. The enzyme dissolved in a 20% molar ratio of the dimethyl sulfoxide-water mixture does not present enzymatic activity. There is preferential solvation of the 1,4-bis-2-ethylhexylsulfosuccinate reverse micelle interface by water molecules. The kinetic parameters are determined at fixed ratio ([water] + [dimethyl sulfoxide])/[1,4-bis-2-ethylhexylsulfosuccinate] = 20 at different dimethyl sulfoxide-water compositions. Michaelis-Menten mechanism is valid for alpha-chymotrypsin in all the reverse micelle systems studied and the reaction takes place at the reverse micelle interface. The enzyme encapsulated by the reverse micelles shows catalytic effects with similar kcat/KM values at any dimethyl sulfoxide composition investigated
tert-Butanol
precipitation of alpha-chymotrypsin in the simultaneous presence of ammonium sulfate and tert-butanol, i.e. three phase partitioning, results in preparations which show self aggregation of the enzyme molecules. The aggregates have irregular shapes and have about 3fold higher catalytic activity than the native enzyme. The aggregates do not differ in lambdamax of fluorescence emission, which is around 340 nm. All the aggregates show higher fluorescence emission intensity. Far-UV and near-UV circular dichroism also show no significant structural changes as compared to the native molecule. HPLC gel filtration gives 14 nm as the diameter for all preparations. Results indicate that hydrophobic interactions were the driving force behind this aggregation
acetonitrile
-
approx. 50% loss of activity after 20 min at 25°C in 70% acetonitrile, complete loss of activity after 20 min at 25°C in 75% acetonitrile, approx. 40% loss of activity after 20 min at 25°C in 95% acetonitrile
dioxane
-
approx. 50% loss of activity after 20 min at 25°C in 20% 1,4-dioxane, complete loss of activity after 20 min at 25°C in 60% 1,4-dioxane, approx. 80% loss of activity after 20 min at 25°C in 95% 1,4-dioxane
Ethanol
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, free enzyme in 80 mM Tris-HCl at pH 7.8, 22 days, complete loss of activity
-
25°C, nanogel-immobilized enzyme, 36 days, about 10% loss of activity
-
25°C, tetrabutylammonium bromide, 2 months, 30% loss of activity
-
4°C, free enzyme in 80 mM Tris-HCl at pH 7.8, 36 days, 16.5% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration
-
purification from an activated homogenate of bovine pancreas by adsorption onto nonsoluble alginate beads. Under all the experimental conditions, the enzyme has a positive net electrical charge, whereas alginate is negatively charged. After performing steps of washing and desorption, chymotrypsin is purified 9times with an enzyme recovery of 62%. The method allows purification with suitable values from a raw sample like pancreas homogenate without a previous clarification step
-
use of Sepharose-immobilized denatured alpha-chymotrypsin for purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
enediyne-amino acid conjugates as potent inhibitors of alpha-chymotrypsin
synthesis
agriculture
-
chymotrypsin and potentially other serine proteases could be attractive candidates for the development of biocatalyst for the control of residual pesticides in the environment and on agricultural products
drug development
-
winged bean chymotrypsin-trypsin inhibitor is a dual inhibitor of both chymotrypsin and trypsin and a promising candidate to study for its insecticidal properties against Helicoverpa armigera and other insect pests
synthesis
-
enzymes are often used in organic solvents for catalyzing organic synthesis. Two enzyme preparations, EPRP (enzyme precipitated and rinsed with n-propanol) and PCMC (protein coated microcrystals) show much higher activities than lyophilized powders in such systems. Both preparations involve precipitation by an organic solvent
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stein, R.L.; Strimpler, A.M.
Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin
Biochemistry
26
2611-2615
1987
Bos taurus
Manually annotated by BRENDA team
Rick, W.
Chymotrypsin
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
1045-1051
1974
Bos taurus
-
Manually annotated by BRENDA team
Ascenzi, P.; Menegatti, E.; Guarneri, M.; Bortolotti, F.; Antonini, E.
Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin
Biochemistry
21
2483-2490
1982
Bos taurus
Manually annotated by BRENDA team
Bolognesi, M.; Pugliese, L.; Gatti, G.; Frigerio, F.; Coda, A.; Antolini, L.; Schnebli, H.P.; Menegatti, E.; Amiconi, G.; Ascenzi, P.
X-ray crystal structute of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution
J. Mol. Recognit.
3
163-168
1990
Bos taurus
Manually annotated by BRENDA team
Capasso, C.; Rizzi, M.; Menegatti, E.; Ascenzi, P.; Bolognesi, M.
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites
J. Mol. Recognit.
10
26-35
1997
Bos taurus
Manually annotated by BRENDA team
Scheidig, A.J.; Hynes, T.R.; Pelletier, L.A.; Wells, J.A.; Kossiakoff, A.A.
Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitors domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities
Protein Sci.
6
1806-1824
1997
Bos taurus
Manually annotated by BRENDA team
Asgeirsson, B.; Bjarnason, J.B.
Structural and kinetic properties of chymotrypsin from atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin
Comp. Biochem. Physiol. B
99B
327-335
1991
Bos taurus, Gadus morhua
Manually annotated by BRENDA team
Al-Ajlan, A.; Bailey, G.S.
Purification and partial characterization of camel anionic chymotrypsin
Arch. Biochem. Biophys.
348
363-368
1997
Bos taurus, Camelus bactrianus
Manually annotated by BRENDA team
Cutruzzola, F.; Ascenzi, P.; Barra, D.; Bolognesi, M.; Menegatti, E.; Sarti, P.; Schnebli, H.P.; Tomova, S.; Amiconi, G.
Selective oxidation of Met-192 in bovine alpha-chymotrypsin. Effect on catalytic and inhibitor binding properties
Biochim. Biophys. Acta
1161
201-208
1993
Bos taurus
Manually annotated by BRENDA team
Carrea, G.; Pasta, P.; Antonini, E.
Purification of chymotrypsin by subunit exchange chromatography on the denatured protein
Biotechnol. Bioeng.
25
1331-1339
1983
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Fioretti, E.; Angeletti, M.; Lupidi, G.; Coletta, M.
Heterotropic modulation of the protease-inhibitor-recognition process. Cations effect the binding properties of alpha-chymotrypsin
Eur. J. Biochem.
225
459-465
1994
Bos taurus
Manually annotated by BRENDA team
Birk, Y.
A trypsin and chymotrypsin inhibitor from groundnuts (Arachis hypogaea)
Methods Enzymol.
45
716-722
1976
Bos taurus
Manually annotated by BRENDA team
Simon, L.M.; Kotorman, M.; Garab, G.; Laczko, I.
Structure and activity of alpha-chymotrypsin and trypsin in aqueous organic media
Biochem. Biophys. Res. Commun.
280
1367-1371
2001
Bos taurus
Manually annotated by BRENDA team
Ye, X.Y.; Ng, T.B.; Rao, P.F.
A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans
Biochem. Biophys. Res. Commun.
289
91-96
2001
Bos taurus
Manually annotated by BRENDA team
Simon, L.M.; Kotorman, M.; Garab, G.; Laczko, I.
Effects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin
Biochem. Biophys. Res. Commun.
293
416-420
2002
Bos taurus
Manually annotated by BRENDA team
Kotorman, M.; Laczko, I.; Szabo, A.; Simon, L.M.
Effects of Ca2+ on catalytic activity and conformation of trypsin and alpha-chymotrypsin in aqueous ethanol
Biochem. Biophys. Res. Commun.
304
18-21
2003
Bos taurus
Manually annotated by BRENDA team
Simon, L.M.; Kotorman, M.; Szabo, A.; Garab, G.; Laczko, I.
Effects of polyethylene glycol on stability of alpha-chymotrypsin in aqueous ethanol solvent
Biochem. Biophys. Res. Commun.
317
610-613
2004
Bos taurus
Manually annotated by BRENDA team
Djurdjevic-Pahl, A.; Hewage, C.; Malthouse, J.P.
13C-NMR study of the inhibition of delta-chymotrypsin by a tripeptide-glyoxal inhibitor
Biochem. J.
362
339-347
2002
Bos taurus
Manually annotated by BRENDA team
Case, A.; Huskey, W.P.; Stein, R.L.
Enzymatic reaction of silent substrates: kinetic theory and application to the serine protease chymotrypsin
Biochemistry
42
4727-4732
2003
Bos taurus
Manually annotated by BRENDA team
Belyaeva, E.A.; Gra, D.V.; Eremeev, N.L.
On the mechanism of interaction of organic solvents with the active site of alpha-chymotrypsin
Biochemistry (Moscow)
67
1032-1036
2002
Bos taurus
Manually annotated by BRENDA team
Wesolowska, O.; Krokoszynska, I.; Krowarsch, D.; Otlewski, J.
Enhancement of chymotrypsin-inhibitor/substrate interactions by 3 M NaCl
Biochim. Biophys. Acta
1545
78-85
2001
Bos taurus
Manually annotated by BRENDA team
Kiczak, L.; Kasztura, M.; Koscielska-Kasprzak, K.; Dadlez, M.; Otlewski, J.
Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI)
Biochim. Biophys. Acta
1550
153-163
2001
Bos taurus
Manually annotated by BRENDA team
Thompson, V.F.; Lawson, K.R.; Barlow, J.; Goll, D.E.
Digestion of mu- and m-calpain by trypsin and chymotrypsin
Biochim. Biophys. Acta
1648
140-153
2003
Bos taurus
Manually annotated by BRENDA team
Poerio, E.; Di Gennaro, S.; Di Maro, A.; Farisei, F.; Ferranti, P.; Parente, A.
Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin
Biol. Chem.
384
295-304
2003
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Smoum, R.; Rubinstein, A.; Srebnik, M.
A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: a subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides
Bioorg. Chem.
31
464-474
2003
Bos taurus
Manually annotated by BRENDA team
Pochet, L.; Doucet, C.; Dive, G.; Wouters, J.; Masereel, B.; Reboud-Ravaux, M.; Pirotte, B.
Coumarinic derivatives as mechanism-based inhibitors of alpha-chymotrypsin and human leukocyte elastase
Bioorg. Med. Chem.
8
1489-1501
2000
Bos taurus
Manually annotated by BRENDA team
Abell, A.D.; Nabbs, B.K.
Ring-deactivated hydroxymethylpyrroles as inhibitors of alpha-chymotrypsin
Bioorg. Med. Chem.
9
621-628
2001
Bos taurus
Manually annotated by BRENDA team
Han, M.S.; Oh, D.J.; Kim, D.H.
Inhibition of alpha-chymotrypsin with thiol-bearing substrate analogues in the presence of zinc ion
Bioorg. Med. Chem. Lett.
14
701-705
2004
Bos taurus
Manually annotated by BRENDA team
Sato, M.; Sasaki, T.; Kobayashi, M.; Kise, H.
Time-dependent structure and activity changes of alpha-chymotrypsin in water/alcohol mixed solvents
Biosci. Biotechnol. Biochem.
64
2552-2558
2000
Bos taurus
Manually annotated by BRENDA team
Fernandez, M.; Villalonga Mde, L.; Fragoso, A.; Cao, R.; Villalonga, R.
Stabilization of alpha-chymotrypsin by modification with beta-cyclodextrin derivatives
Biotechnol. Appl. Biochem.
36
235-239
2002
Bos taurus
Manually annotated by BRENDA team
Fadnavis, N.W.; Bhaskar, V.; Kantam, M.L.; Choudary, B.M.
Highly efficient "tight fit" immobilization of alpha-chymotrypsin in mesoporous MCM-41: a novel approach using precursor immobilization and activation
Biotechnol. Prog.
19
346-351
2003
Bos taurus
Manually annotated by BRENDA team
Gunther, R.; Thust, S.; Hofmann, H.J.; Bordusa, F.
Trypsin-specific acyl-4-guanidinophenyl esters for alpha-chymotrypsin-catalysed reactions computational predictions, hydrolyses, and peptide bond formation
Eur. J. Biochem.
267
3496-3501
2000
Bos taurus
Manually annotated by BRENDA team
Spreti, N.; Di Profio, P.; Marte, L.; Bufali, S.; Brinchi, L.; Savelli, G.
Activation and stabilization of alpha-chymotrypsin by cationic additives
Eur. J. Biochem.
268
6491-6497
2001
Bos taurus
Manually annotated by BRENDA team
Yakoby, N.; Raskin, I.
A simple method to determine trypsin and chymotrypsin inhibitory activity
J. Biochem. Biophys. Methods
59
241-251
2004
Bos taurus
Manually annotated by BRENDA team
Roussel, A.; Mathieu, M.; Dobbs, A.; Luu, B.; Cambillau, C.; Kellenberger, C.
Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity
J. Biol. Chem.
276
38893-38898
2001
Bos taurus
Manually annotated by BRENDA team
O'Malley, K.M.; Cooperman, B.S.
Formation of the covalent chymotrypsin.antichymotrypsin complex involves no large-scale movement of the enzyme
J. Biol. Chem.
276
6631-6639
2001
Bos taurus
Manually annotated by BRENDA team
Kolodziej, S.J.; Wagenknecht, T.; Strickland, D.K.; Stoops, J.K.
The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes
J. Biol. Chem.
277
28031-28037
2002
Bos taurus
Manually annotated by BRENDA team
Chopin, V.; Stefano, G.; Salzet, M.
Biochemical evidence of specific trypsin-chymotrypsin inhibitors in the rhynchobdellid leech, Theromyzon tessulatum
J. Enzyme Inhib.
15
367-379
2000
Bos taurus
Manually annotated by BRENDA team
Ghani, U.; Ng, K.K.; Atta ur, R.; Choudhary, M.I.; Ullah, N.; James, M.N.
Crystal structure of gamma-chymotrypsin in complex with 7-hydroxycoumarin
J. Mol. Biol.
314
519-525
2001
Bos taurus (P00766)
Manually annotated by BRENDA team
Al-Ajlan, A.; Bailey, G.S.
Purification and characterization of cationic chymotrypsin from the pancreas of the Arabian camel (Camelus dromedarius)
Mol. Cell. Biochem.
203
73-78
2000
Bos taurus, Camelus dromedarius
Manually annotated by BRENDA team
Komada, A.; Yamauchi, Y.; Ikesue, K.; Fujita, T.; Nose, T.; Sakaguchi, K.; Shimohigashi, Y.
Characteristic intra- and intermolecular interactions of dipeptide-chymotrypsin complex as specific structural essentials for enzyme inhibition
Pept. Sci.
38
179-182
2002
Bos taurus
-
Manually annotated by BRENDA team
Rajic, A.; Akihisa, T.; Ukiya, M.; Yasukawa, K.; Sandeman, R.M.; Chandler, D.S.; Polya, G.M.
Inhibition of trypsin and chymotrypsin by anti-inflammatory triterpenoids from Compositae flowers
Planta Med.
67
599-604
2001
Bos taurus
Manually annotated by BRENDA team
Fischer, N.O.; McIntosh, C.M.; Simard, J.M.; Rotello, V.M.
Inhibition of chymotrypsin through surface binding using nanoparticle-based receptors
Proc. Natl. Acad. Sci. USA
99
5018-5023
2002
Bos taurus
Manually annotated by BRENDA team
Celej, M.S.; Dandrea, M.G.; Campana, P.T.; Fidelio, G.D.; Bianconi, M.L.
Superactivity and conformational changes on alpha-chymotrypsin upon interfacial binding to cationic micelles
Biochem. J.
378
1059-1066
2004
Bos taurus
Manually annotated by BRENDA team
Hengge, A.C.; Stein, R.L.
Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates
Biochemistry
43
742-747
2004
Bos taurus
Manually annotated by BRENDA team
Tardioli, P.W.; Sousa, R.J.; Giordano, R.C.; Giordano, R.L.
Kinetic model of the hydrolysis of polypeptides catalyzed by alcalase immobilized on 10% glyoxyl-agarose
Enzyme Microb. Technol.
36
555-564
2005
Bos taurus
-
Manually annotated by BRENDA team
Singh, N.; Jabeen, T.; Sharma, S.; Roy, I.; Gupta, M.N.; Bilgrami, S.; Somvanshi, R.K.; Dey, S.; Perbandt, M.; Betzel, C.; Srinivasan, A.; Singh, T.P.
Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution
FEBS J.
272
562-572
2005
Bos taurus
Manually annotated by BRENDA team
Abuin, E.; Lissi, E.; Duarte, R.
Kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by alpha-chymotrypsin in aqueous solutions of dodecyltrimethylammonium bromide
J. Colloid Interface Sci.
283
539-543
2005
Bos taurus
Manually annotated by BRENDA team
Czapinska, H.; Helland, R.; Smalas, A.O.; Otlewski, J.
Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants
J. Mol. Biol.
344
1005-1020
2004
Bos taurus
Manually annotated by BRENDA team
Thompson, S.; Fawcett, M.C.; Pulman, L.B.; Self, C.H.
A simple procedure for the photoregulation of chymotrypsin activity
Photochem. Photobiol. Sci.
5
326-330
2006
Bos taurus
Manually annotated by BRENDA team
Matrai, J.; Verheyden, G.; Krueger, P.; Engelborghs, Y.
Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide
Protein Sci.
13
3139-3150
2004
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Esteves, G.F.; Teles, R.C.; Cavalcante, N.S.; Neves, D.; Ventura, M.M.; Barbosa, J.A.; de Freitas, S.M.
Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex
Acta Crystallogr. Sect. F
63
1087-1090
2007
Bos taurus (P00766)
Manually annotated by BRENDA team
Spink, E.; Hewage, C.; Malthouse, J.P.
Determination of the structure of tetrahedral transition state analogues bound at the active site of chymotrypsin using 18O and 2H isotope shifts in the 13C NMR spectra of glyoxal inhibitors
Biochemistry
46
12868-12874
2007
Bos taurus
Manually annotated by BRENDA team
Moulin, A.; Bell, J.H.; Pratt, R.F.; Ringe, D.
Inhibition of chymotrypsin by a complex of ortho-vanadate and benzohydroxamic acid: structure of the inert complex and its mechanistic interpretation
Biochemistry
46
5982-5990
2007
Bos taurus (P00766)
Manually annotated by BRENDA team
Rezaei-Ghaleh, N.; Ramshini, H.; Ebrahim-Habibi, A.; Moosavi-Movahedi, A.A.; Nemat-Gorgani, M.
Thermal aggregation of alpha-chymotrypsin: role of hydrophobic and electrostatic interactions
Biophys. Chem.
132
23-32
2008
Bos taurus
Manually annotated by BRENDA team
You, C.; Arvizo, R.R.; Rotello, V.M.
Regulation of alpha-chymotrypsin activity on the surface of substrate-functionalized gold nanoparticles
Chem. Commun. (Camb. )
2006
2905-2907
2006
Bos taurus
-
Manually annotated by BRENDA team
Rezaei-Ghaleh, N.; Ebrahim-Habibi, A.; Moosavi-Movahedi, A.A.; Nemat-Gorgani, M.
Effect of polyamines on the structure, thermal stability and 2,2,2-trifluoroethanol-induced aggregation of alpha-chymotrypsin
Int. J. Biol. Macromol.
41
597-604
2007
Bos taurus
Manually annotated by BRENDA team
Chicon, R.; Lopez-Fandino, R.; Quiros, A.; Belloque, J.
Changes in chymotrypsin hydrolysis of beta-lactoglobulin A induced by high hydrostatic pressure
J. Agric. Food Chem.
54
2333-2341
2006
Bos taurus
Manually annotated by BRENDA team
Spink, E.; Cosgrove, S.; Rogers, L.; Hewage, C.; Malthouse, J.P.
13C and 1H NMR studies of ionizations and hydrogen bonding in chymotrypsin-glyoxal inhibitor complexes
J. Biol. Chem.
282
7852-7861
2007
Bos taurus
Manually annotated by BRENDA team
Tubio, G.; Nerli, B.; Pico, G.
Partitioning features of bovine trypsin and alpha-chymotrypsin in polyethyleneglycol-sodium citrate aqueous two-phase systems
J. Chromatogr. B
852
244-249
2007
Bos taurus
Manually annotated by BRENDA team
Abuin, E.; Lissi, E.; Calderon, C.
Kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by alpha-chymotrypsin in aqueous solutions of alkyltrimethylammonium bromides
J. Colloid Interface Sci.
308
573-576
2007
Bos taurus
Manually annotated by BRENDA team
Hong, J.; Xu, D.; Gong, P.; Sun, H.; Dong, L.; Yao, S.
Covalent binding of alpha-chymotrypsin on the magnetic nanogels covered by amino groups
J. Mol. Catal. B
45
84-90
2007
Bos taurus
-
Manually annotated by BRENDA team
Spreti, N.; Mancini, M.V.; Germani, R.; Di Profio, P.; Savelli, G.
Substrate effect on alpha-chymotrypsin activity in aqueous solutions of "big-head" ammonium salts
J. Mol. Catal. B
50
1-6
2008
Bos taurus
-
Manually annotated by BRENDA team
Okamura, M.; Yokoyama, N.; Takabatake, N.; Okubo, K.; Ikehara, Y.; Igarashi, I.
Modification of host erythrocyte membranes by trypsin and chymotrypsin treatments and effects on the in vitro growth of bovine and equine Babesia parasites
J. Parasitol.
93
208-211
2007
Bos taurus
Manually annotated by BRENDA team
Banerjee, D.; Srivastava, S.K.; Pal, S.K.
Spectroscopic studies on ligand-enzyme interactions: complexation of alpha-chymotrypsin with 4,6-diamidino-2-phenylindole (DAPI)
J. Phys. Chem. B
112
1828-1833
2008
Bos taurus (P00766)
Manually annotated by BRENDA team
Wysocka, M.; Lesner, A.; Legowska, A.; Ja?kiewicz, A.; Miecznikowska, H.; Rolka, K.
Designing of substrates and inhibitors of bovine alpha-chymotrypsin with synthetic phenylalanine analogues in position P(1)
Protein Pept. Lett.
15
260-264
2008
Bos taurus
Manually annotated by BRENDA team
Lopes, A.R.; Sato, P.M.; Terra, W.R.
Insect chymotrypsins: chloromethyl ketone inactivation and substrate specificity relative to possible coevolutional adaptation of insects and plants
Arch. Insect Biochem. Physiol.
70
188-203
2009
Bos taurus, Tenebrio molitor, Diatraea saccharalis, Periplaneta americana (Q1M0X9), Spodoptera frugiperda (Q86M89), Spodoptera frugiperda
Manually annotated by BRENDA team
Adriano, W.S.; Mendonca, D.B.; Rodrigues, D.S.; Mammarella, E.J.; Giordano, R.L.
Improving the properties of chitosan as support for the covalent multipoint immobilization of chymotrypsin
Biomacromolecules
9
2170-2179
2008
Bos taurus
Manually annotated by BRENDA team
Legowska, A.; Debowski, D.; Lesner, A.; Wysocka, M.; Rolka, K.
Introduction of non-natural amino acid residues into the substrate-specific P(1) position of trypsin inhibitor SFTI-1 yields potent chymotrypsin and cathepsin G inhibitors
Bioorg. Med. Chem.
17
3302-3307
2009
Bos taurus
Manually annotated by BRENDA team
Rezaei-Ghaleh, N.; Zweckstetter, M.; Morshedi, D.; Ebrahim-Habibi, A.; Nemat-Gorgani, M.
Amyloidogenic potential of alpha-chymotrypsin in different conformational states
Biopolymers
91
28-36
2009
Bos taurus (P00766)
Manually annotated by BRENDA team
Rodriguez-Martinez, J.A.; Sola, R.J.; Castillo, B.; Cintron-Colon, H.R.; Rivera-Rivera, I.; Barletta, G.; Griebenow, K.
Stabilization of alpha-chymotrypsin upon PEGylation correlates with reduced structural dynamics
Biotechnol. Bioeng.
101
1142-1149
2008
Bos taurus
Manually annotated by BRENDA team
Pham, V.T.; Ewing, E.; Kaplan, H.; Choma, C.; Hefford, M.A.
Glycation improves the thermostability of trypsin and chymotrypsin
Biotechnol. Bioeng.
101
452-459
2008
Bos taurus
Manually annotated by BRENDA team
Rodriguez-Martinez, J.A.; Rivera-Rivera, I.; Sola, R.J.; Griebenow, K.
Enzymatic activity and thermal stability of PEG-alpha-chymotrypsin conjugates
Biotechnol. Lett.
31
883-887
2009
Bos taurus
Manually annotated by BRENDA team
Solanki, K.; Gupta, M.N.
Optimising biocatalyst design for obtaining high transesterification activity by alpha-chymotrypsin in non-aqueous media
Chem. Cent. J.
2
2
2008
Bos taurus
Manually annotated by BRENDA team
Demaneche, S.; Chapel, J.P.; Monrozier, L.J.; Quiquampoix, H.
Dissimilar pH-dependent adsorption features of bovine serum albumin and alpha-chymotrypsin on mica probed by AFM
Colloids Surf. B Biointerfaces
70
226-231
2009
Bos taurus
Manually annotated by BRENDA team
Zelazko, M.; Chrzanowska, J.; Polanowski, A.
Pancreatic proteolytic enzymes of ostrich purified on immobilized protein inhibitors. Characterization of a new form of chymotrypsin (Chtr1)
Comp. Biochem. Physiol. B
151
102-109
2008
Bos taurus, Struthio camelus
Manually annotated by BRENDA team
Telang, M.A.; Giri, A.P.; Pyati, P.S.; Gupta, V.S.; Tegeder, M.; Franceschi, V.R.
Winged bean chymotrypsin inhibitors retard growth of Helicoverpa armigera
Gene
431
80-85
2009
Bos taurus
Manually annotated by BRENDA team
Ju, H.Y.; Too, J.R.; Chang, C.; Shieh, C.J.
Optimal alpha-chymotrypsin-catalyzed synthesis of N-Ac-Phe-Gly-NH(2)
J. Agric. Food Chem.
57
403-408
2009
Bos taurus
Manually annotated by BRENDA team
Venkatesu, P.; Lee, M.J.; Lin, H.M.
Osmolyte Counteracts Urea-Induced Denaturation of alpha-Chymotrypsin
J. Phys. Chem. B
113
5327-5338
2009
Bos taurus (P00766)
Manually annotated by BRENDA team
Banerjee, D.; Pal, S.K.
Conformational dynamics at the active site of alpha-chymotrypsin and enzymatic activity
Langmuir
24
8163-8168
2008
Bos taurus
Manually annotated by BRENDA team
Ye, X.; Bun Ng, T.
A trypsin-chymotrypsin inhibitor with antiproliferative activity from small glossy black soybeans
Planta Med.
75
550-556
2009
Bos taurus
Manually annotated by BRENDA team
Cheung, A.H.; Wong, J.H.; Ng, T.B.
Trypsin-chymotrypsin inhibitors from Vigna mungo seeds
Protein Pept. Lett.
16
277-284
2009
Bos taurus
Manually annotated by BRENDA team
Lesner, A.; Wysocka, M.; Solek, M.; Legowska, A.; Rolka, K.
Low-molecular-weight aldehyde inhibitors of cathepsin g
Protein Pept. Lett.
16
408-410
2009
Bos taurus
Manually annotated by BRENDA team
Yang, Q.; Sun, L.; Zhang, D.; Qian, J.; Sun, Y.; Ma, L.; Sun, J.; Hu, X.; Tan, W.; Wang, W.; Zhu, C.
Partial characterization of deltamethrin metabolism catalyzed by chymotrypsin
Toxicol. In Vitro
22
1528-1533
2008
Bos taurus
Manually annotated by BRENDA team
Bruni, N.; Di Maro, A.; Costantini, S.; Chambery, A.; Facchiano, A.M.; Ficca, A.G.; Parente, A.; Poerio, E.
Redesigning the reactive site loop of the wheat subtilisin/chymotrypsin inhibitor (WSCI) by site-directed mutagenesis. A protein-protein interaction study by affinity chromatography and molecular modeling
Biochimie
91
1112-1122
2009
Bos taurus
Manually annotated by BRENDA team
Dutta, S.; Basak, A.; Dasgupta, S.
Design and synthesis of enediyne-peptide conjugates and their inhibiting activity against chymotrypsin
Bioorg. Med. Chem.
17
3900-3908
2009
Bos taurus (P00766)
Manually annotated by BRENDA team
Roy, S.; Dutta, S.K.
Genomic and cDNA cloning, expression, purification, and characterization of chymotrypsin-trypsin inhibitor from winged bean seeds
Biosci. Biotechnol. Biochem.
73
2671-2676
2009
Bos taurus
Manually annotated by BRENDA team
Castillo-Yanez, F.; Pacheco-Aguilar, R.; Lugo-Sanchez, M.; Garcia-Sanchez, G.; Quintero-Reyes, I.
Biochemical characterization of an isoform of chymotrypsin from the viscera of Monterey sardine (Sardinops sagax caerulea), and comparison with bovine chymotrypsin
Food Chem.
112
634-639
2009
Bos taurus, Sardinops caeruleus
Manually annotated by BRENDA team
Yang, F.; Su, W.; Lu, B.; Wu, T.; Sun, L.; Hara, K.; Cao, M.
Purification and characterization of chymotrypsins from the hepatopancreas of crucian carp (Carassius auratus)
Food Chem.
116
860-866
2009
Bos taurus, Carassius auratus
Manually annotated by BRENDA team
Pietrusewicz, E.; Sienczyk, M.; Oleksyszyn, J.
Novel diphenyl esters of peptidyl alpha-aminoalkylphosphonates as inhibitors of chymotrypsin and subtilisin
J. Enzyme Inhib. Med. Chem.
24
1229-1236
2009
Bos taurus
Manually annotated by BRENDA team
Bayindir, Z.S.; Yuksel, N.
Characterization of niosomes prepared with various nonionic surfactants for paclitaxel oral delivery
J. Pharm. Sci.
99
2049-2060
2010
Bos taurus
Manually annotated by BRENDA team
Raju, S.; Jayalakshmi, S.K.; Sreeramulu, K.
Differential elicitation of proteases and protease inhibitors in two different genotypes of chickpea (Cicer arietinum) by salicylic acid and spermine
J. Plant Physiol.
166
1015-1022
2009
Bos taurus
Manually annotated by BRENDA team
Lopes, J.L.; Valadares, N.F.; Moraes, D.I.; Rosa, J.C.; Araujo, H.S.; Beltramini, L.M.
Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa
Phytochemistry
70
871-879
2009
Bos taurus
Manually annotated by BRENDA team
Lazar, L.M.; Fisher, S.Z.; Moulin, A.G.; Kovalevsky, A.; Novak, W.R.; Langan, P.; Petsko, G.A.; Ringe, D.
Time-of-flight neutron diffraction study of bovine gamma-chymotrypsin at the Protein Crystallography Station
Acta Crystallogr. Sect. F
67
587-590
2011
Bos taurus (P00766)
Manually annotated by BRENDA team
Cummings, C.; Murata, H.; Koepsel, R.; Russell, A.J.
Dramatically increased pH and temperature stability of chymotrypsin using dual block polymer-based protein engineering
Biomacromolecules
15
763-771
2014
Bos taurus (P00766)
Manually annotated by BRENDA team
Verma, S.; Ghosh, K.; Verma, R.; Xiang, W.; Li, N.; Zhao, X.
Surface, conformational and catalytic activity approach of alpha-chymotrypsin and trypsin in micellar media
Colloids Surf. A Physicochem. Eng. Asp.
470
188-193
2015
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Cunha, E.; Passos, M.L.; Pinto, P.C.; Saraiva, M.L.
Improved activity of alpha-chymotrypsin in mixed micelles of cetyltrimethylammonium bromide (CTAB) and ionic liquids: a kinetic study resorting to sequential injection analysis
Colloids Surf. B Biointerfaces
118
172-178
2014
Bos taurus (P00766)
Manually annotated by BRENDA team
Verma, S.; Ghosh, K.
Activity, stability and kinetic parameters for alpha-chymotrypsin catalysed reactions in AOT/isooctane reverse micelles with nonionic and zwitterionic mixed surfactants
J. Chem. Sci.
125
875-882
2013
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Paulus, A.; Morhardt, C.; Lehle, N.; Franzreb, M.
Recovery of chymotrypsin using magnetic particles and aqueous micellar two-phase systems: Influence of non-ionic surfactants on enzyme activity
J. Mol. Catal. B
110
165-170
2014
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Valiullina, Y.; Ermakova, E.; Faizullin, D.; Mirgorodskaya, A.; Zuev, Y.
Structure and properties of complexes of α-chymotrypsin with hydroxyl-containing gemini dicationic surfactants with a spacer moiety of varying length
J. Struct. Chem.
55
1556-1564
2014
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Verma, S.; Ghosh, K.
Effect of cationic surfactants on the enzymatic activity of alpha-chymotrypsin
Kinet. Catal.
52
6-10
2011
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Moyano, F.; Setien, E.; Silber, J.J.; Correa, N.M.
Enzymatic hydrolysis of N-benzoyl-L-tyrosine p-nitroanilide by ?-chymotrypsin in DMSO-water/AOT/n-heptane reverse micelles. A unique interfacial effect on the enzymatic activity
Langmuir
29
8245-8254
2013
Bos taurus (P00766)
Manually annotated by BRENDA team
Perveen, S.; Mustafa, S.; Latif, M.; Iqbal, L.; Usmani, T.; Khan, K.; Voelter, W.
Unsymmetrical 1,3-disubstituted urea derivatives as alpha-chymotrypsin inhibitors
Med. Chem. Res.
23
3585-3592
2014
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Rather, G.M.; Mukherjee, J.; Halling, P.J.; Gupta, M.N.
Activation of alpha chymotrypsin by three phase partitioning is accompanied by aggregation
PLoS ONE
7
e49241
2012
Bos taurus (P00766)
Manually annotated by BRENDA team
Spelzini, D.; Farruggia, B.; Pico, G.
Purification of chymotrypsin from pancreas homogenate by adsorption onto non-soluble alginate beads
Process Biochem.
46
801-805
2011
Bos taurus
-
Manually annotated by BRENDA team
Plyushchenko, A.; Borovikova, L.; Pisarev, O.
Proteolytic activity of chymotrypsin immobilized on selenium nanoparticles
Appl. Biochem. Microbiol.
54
375-378
2018
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Marasini, B.P.; Rahim, F.; Perveen, S.; Karim, A.; Mohammed Khan, K.; Atta-Ur-Rahman, K.; Choudhary, M.I.
Synthesis, structure-activity relationships studies of benzoxazinone derivatives as alpha-chymotrypsin inhibitors
Bioorg. Chem.
70
210-221
2017
Bos taurus (P00766)
Manually annotated by BRENDA team
Schuabb, V.; Winter, R.; Czeslik, C.
Improved activity of alpha-chymotrypsin on silica particles - A high-pressure stopped-flow study
Biophys. Chem.
218
1-6
2016
Bos taurus (P00766)
Manually annotated by BRENDA team
Yoshimoto, M.; Yamada, J.; Baba, M.; Walde, P.
Enhanced heat stability of alpha-chymotrypsin through single-enzyme confinement in Attoliter liposomes
ChemBioChem
17
1221-1224
2016
Bos taurus (P00766)
Manually annotated by BRENDA team
Vorobev, M.; Kochetkov, K.
Determination of kinetic parameters for casein hydrolysis by chymotrypsin using two ranges of substrate concentration
Int. Dairy J.
61
76-84
2016
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Asgharzadeh, S.; Shareghi, B.; Farhadian, S.
Experimental and theoretical investigations on the interaction of L-methionine molecules with alpha-chymotrypsin in the aqueous solution using various methods
Int. J. Biol. Macromol.
131
548-556
2019
Bos taurus (P00766)
Manually annotated by BRENDA team
Wang, J.; Zheng, X.; Wang, W.; Guo, H.; Liu, R.; Zong, W.
A study on the interaction between cadmium and alpha-chymotrypsin and the underlying mechanisms
J. Biochem. Mol. Toxicol.
33
e22248
2019
Bos taurus (P00766)
Manually annotated by BRENDA team
Farhadian, S.; Shareghi, B.; Saboury, A.A.
Exploring the thermal stability and activity of alpha-chymotrypsin in the presence of spermine
J. Biomol. Struct. Dyn.
35
435-448
2017
Bos taurus (P00766)
Manually annotated by BRENDA team
Patra, A.; Samanta, N.; Das, D.K.; Mitra, R.K.
Enhanced catalytic activity of alpha-chymotrypsin in cationic surfactant solutions the component specificity revisited
J. Phys. Chem. B
121
1457-1465
2017
Bos taurus (P00766)
Manually annotated by BRENDA team
Mazur-Marzec, H.; Fidor, A.; Ceglowska, M.; Wieczerzak, E.; Kropidlowska, M.; Goua, M.; Macaskill, J.; Edwards, C.
Cyanopeptolins with trypsin and chymotrypsin inhibitory activity from the cyanobacterium Nostoc edaphicum CCNP1411
Mar. Drugs
16
E220
2018
Bos taurus (P00766)
Manually annotated by BRENDA team
Komissarov, I.; Kuchierskaya, A.; Sirotkin, V.
Residual activity of alpha-chymotrypsin in water-1,2-propanediol mixtures
Organic Solvents: Properties Applications and Health Effects
1
73-91
2017
Bos taurus (P00766)
-
Manually annotated by BRENDA team
Bahamondes, C.; Alvaro, G.; Wilson, L.; Illanes, A.
Effect of enzyme load and catalyst particle size on the diffusional restrictions in reactions of synthesis and hydrolysis catalyzed by alpha-chymotrypsin immobilized into glyoxal-agarose
Process Biochem.
53
172-179
2017
Bos taurus (P00766)
-
Manually annotated by BRENDA team
De Matteis, L.; Di Renzo, F.; Germani, R.; Goracci, L.; Spreti, N.; Tiecco, M.
alpha-Chymotrypsin superactivity in quaternary ammonium salt solution Kinetic and computational studies
RSC Adv.
6
46202-46211
2016
Bos taurus (P00766)
-
Manually annotated by BRENDA team