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2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
L-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
N-benzoyl-L-tyrosine 4-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine-4-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
-
-
-
?
N-benzoyl-L-tyrosyl-ethyl ester + H2O
?
-
-
-
?
N-glutaryl-L-phenylalanine-4-nitroanilide + H2O
N-glutaryl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
?
N-succinyl-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Gly-Gly-4-nitroanilide + H2O
N-succinyl-Gly-Gly + 4-nitroaniline
-
-
-
?
N-succinyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
-
-
-
?
2-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]ethanaminium + H2O
?
-
-
-
-
?
4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoic acid + H2O
?
-
-
-
-
?
4-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]butanoate + H2O
?
-
-
-
-
?
acetyl-L-Leu methyl ester + H2O
acetyl-L-Leu + methanol
-
-
-
-
?
acetyl-L-Trp ethyl ester + H2O
acetyl-L-Trp + ethanol
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
?
benzoyl-4-guanidinophenyl ester + H2O
benzoyl + 4-guanidinophenol
-
-
-
?
benzoyl-D-Ala-4-guanidinophenyl ester + H2O
benzoyl-D-Ala + 4-guanidinophenol
-
5% of activity with N-benzoyl-L-Ala-4-guanidinophenyl ester
-
?
benzoyl-D-Leu-4-guanidinophenyl ester + H2O
benzoyl-D-Leu + 4-guanidinophenol
-
-
-
?
benzoyl-D-Phe-4-guanidinophenyl ester + H2O
benzoyl-D-Phe + 4-guanidinophenol
-
-
-
?
benzoyl-Gly-4-guanidinophenyl ester + H2O
benzoyl-Gly + 4-guanidinophenol
-
-
-
?
benzoyl-L-Ala-4-guanidinophenyl ester + H2O
benzoyl-L-Ala + 4-guanidinophenol
-
-
-
?
benzoyl-L-tyrosine ethyl ester + H2O
?
-
-
-
-
?
benzoyl-Tyr-p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
-
-
-
?
benzoyl-tyrosine p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
-
-
-
?
beta-lactoglobulin A + H2O
?
-
-
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
?
-
-
-
-
?
bovine serum albumine + H2O
?
-
-
-
-
?
casein + H2O
fragments of casein
cheese whey protein + H2O
?
-
-
-
-
r
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
-
1 mM in 25mM Tris-HCl buffer containing 0.5M NaCl
-
-
?
L-Tyr ethyl ester + H2O
L-Tyr + ethanol
-
-
-
-
?
m-calpain + H2O
fragments of m-calpain
-
-
-
?
mu-calpain + H2O
fragments of mu-calpain
-
-
-
?
N-acetyl-DL-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-DL-Phe-beta-naphthylester + H2O
N-acetyl-DL-Phe + beta-naphthol
-
-
-
?
N-acetyl-DL-phenylglycine methyl ester + H2O
N-acetyl-L-phenylglycine + methanol
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-L-leucine methyl ester + H2O
N-acetyl-L-leucine + methanol
-
5% of kcat with N-acetyl-L-tyrosine ethyl ester
-
?
N-acetyl-L-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + glycinamide
N-Ac-Phe-Gly-NH2 + ethanol
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + H2O
N-acetyl-L-phenylalanine + ethanol
-
-
-
?
N-acetyl-L-tryptophan ethyl ester + H2O
N-acetyl-L-tryptophan + ethanol
-
-
-
?
N-acetyl-L-Tyr ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
-
-
?
N-acetyl-L-Tyr-ethyl ester + H2O
N-acetyl-L-Tyr + ethanol
-
-
-
?
N-acetyl-L-Tyr-p-nitroanilide + H2O
N-acetyl-L-Tyr + p-nitroaniline
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
N-alpha-acetyl-L-tyrosine ethyl ester + H2O
N-alpha-acetyl-L-tyrosine + ethanol
-
-
-
?
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
? + p-nitroaniline
-
BApNA
-
-
?
N-alpha-benzoyl-L-tyrosine ethyl ester + H2O
?
-
-
-
-
?
N-alpha-benzoyl-L-tyrosyl ethyl ester + H2O
?
-
-
-
-
?
N-benzoyl-L-arginine ethyl ester + H2O
N-benzoyl-L-arginine + ethanol
-
0.5 mM in 50 mM phosphate buffer, pH 7.6
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
N-benzoyl-L-Tyr-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
N-benzoyl-L-tyrosine ethyl ester + methanol
N-benzoyl-L-tyrosine methyl ester + ethanol
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + ethanol
N-benzoyl-L-tyrosine ethyl ester + methanol
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + H2O
N-benzoyl-L-tyrosine + methanol
-
-
-
?
N-benzoyl-L-tyrosine p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
-
-
?
N-benzoyl-Tyr p-nitroanilide + H2O
N-benzoyl-Tyr + p-nitroaniline
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
N-glutamyl-L-phenylalanine p-nitroanilide + H2O
p-nitroaniline + N-glutamyl-L-phenylalanine
-
-
-
-
?
N-glutaryl-L-Phe-p-nitroanilide + H2O
N-glutaryl-L-Phe + p-nitroaniline
-
-
-
?
N-glutaryl-L-phenylalanine-p-nitroanilide + H2O
N-glutaryl-L-phenylalanine + p-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Ala p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Arg + p-nitroaniline
-
very low activity
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Lys + p-nitroaniline
-
extremly low activity
-
?
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nle + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nva + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
N-succinyl-Ala-Phe-Ala + H2O
N-succinyl-Ala-Phe + alanine
-
-
-
?
N-succinyl-Ala-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Phe + p-nitroaniline
-
-
-
?
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
N-succinyl-L-phenylalanine p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
-
-
-
-
?
N-succinyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Phe-p-nitroanilide + H2O
p-nitroaniline + N-succinyl-Phe
-
-
-
-
?
N-[1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]-N'-[2-[2-(2-hydroxyethoxy)ethoxy]ethyl]butanediamide + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Ala + p-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Leu p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Leu + p-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + p-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Tyr + p-nitrophenol
-
-
-
-
?
Nalpha-tosyl-L-Tyr benzyl ester + H2O
Nalpha-tosyl-L-Tyr + phenol
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
succinimidyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinimidyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + p-nitroaniline
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-Thr-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Z-Phe-Arg-Thr-Tyr + 5-amino-2-nitrobenzamide
-
-
-
-
?
additional information
?
-
casein + H2O
fragments of casein
-
-
-
?
casein + H2O
fragments of casein
-
-
-
?
casein + H2O
fragments of casein
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
-
alpha-chymotrypsin immobilized to mesoporous silica
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
SucAAPFpNA
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
-
-
-
-
?
additional information
?
-
a variety of experimental methods, including fluorescence emission, dynamic quenching, steady-state fluorescence anisotropy, far-UV circular dichroism, nuclear magnetic resonance spectroscopy, and dynamic light scattering are employed to characterize the conformational states of achymotrypsin that precede formation of amyloid fibrils
-
-
?
additional information
?
-
-
chymotrypsin cleaves a number of detectable membrane proteins of bovine and equine erythrocytes (at least 87000 Da, 71000 Da and 33000 Da fragments)
-
-
?
additional information
?
-
-
specificity of Chtr1 reactive site is determined by hydrolysis of the oxidized bovine insulin B-chain
-
-
?
additional information
?
-
-
chymotrypsin cleaves peptides at the carboxyl side of aromatic rings. Niosomal encapsulation by nonionic surfactant based vesicles protects the antineoplastic agent Paclitaxel from chymotrypsin degradation
-
-
?
additional information
?
-
-
chymotrypsin does not reveal activity against gelatin
-
-
?
additional information
?
-
-
mutant Y50G of the wheat subtilisin/chymotrypsin inhibitor acts as a common substrate for chymotrypsin
-
-
?
additional information
?
-
-
N-alpha-benzoyl-DL-arginine p-nitroanilide synthetic substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
-
basic pancreatic trypsin inhibitor
-
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
-
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
-
-
faradiol 3-O-myristate
-
0.000032 mM, 50% inhibition, noncompetitive inhibition
faradiol 3-O-palmitate
-
0.000072 mM, 50% inhibition, noncompetitive inhibition
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
-
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
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
basic pancreatic trypsin inhibitor
-
-
-
basic pancreatic trypsin inhibitor
-
engineering of inhibitors with altered specificities
-
basic pancreatic trypsin inhibitor
-
moderate inhibition at pH 8.3, mutants of basic pancreatic trypsin inhibitor, i.e. BPTI, that strongly inhibit alpha-chymotrypsin are obtained by affinity selection of an M13 phage displayed library of BPTI variants
-
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
-
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
extremely potent inhibitor
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits (17% residual activity)
-
additional information
not inhibited by 4',6-diamidino-2-phenylindole
-
additional information
novel synthesized enediyne-amino acid conjugates effectively target chymotrypsin inhibiting its proteolytic activity. Mode of inhibition is mostly competitive or of a mixed type depending on the nature of the inhibitor
-
additional information
inhibitory activity of the urea compounds synthesized depends upon the position of the methyl group at the phenyl ring and the presence of substituents at the nitrogen of the urea bridge. The inhibitory trend suggests that alpha-chymotrypsin inhibitory activity declines with ortho, meta, para substitution order
-
additional information
-
an inhibitor from Arachis hypogaea
-
additional information
-
protease inhibitor does not exert any inhibitory effect on hepatoma (Hep G2) and breast cancer (MCF 7) cells or antifungal action toward Botrytis cinerea, Fusarium oxysporum and Mycosphaerella arachidicola
-
additional information
-
at 25°C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, is not inhibited by benzamidine and EDTA
-
additional information
-
chymotrypsin inhibitory activity of protease inhibitor extract of chickpea resistant cultivar treated with salicylic acid and spermine, respectively, is increased by 92 UI/microg protein (52% over control), 72 UI/microg protein (38% over control) in roots and 79 UI/microg protein (63% over control), 66 UI/microg protein (57% over control) in shoots compared with their respective controls, whereas protease inhibitor extract of susceptible cultivar roots and shoots show 20-30% increase in chymotrypsin inhibitory activity over their respective controls
-
additional information
-
substitution of the phosphonate diphenyl ester rings by a variety of different substituents at different positions does not significantly improve inhibitory activity
-
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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
0.5
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 20, pH 7.8, 27°C
0.7
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 20, pH 7.8, 27°C
0.7
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 10, pH 7.8, 27°C
0.7
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 5, pH 7.8, 27°C
0.82
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 5, pH 7.8, 27°C
1.4
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 10, pH 7.8, 27°C
0.032
4-nitrophenyl benzoate
presence of 2.0 mM cetyltributylphosphonium bromide, pH 7.8, 27°C
0.035
4-nitrophenyl benzoate
presence of 2.0 mM cetyltrimethylammonium bromide, pH 7.8, 27°C
0.048
4-nitrophenyl benzoate
presence of 0.5 mM cetyltributylphosphonium bromide, pH 7.8, 27°C
0.053
4-nitrophenyl benzoate
pH 7.8, 27°C
0.06
4-nitrophenyl benzoate
presence of 0.5 mM cetyltrimethylammonium bromide, pH 7.8, 27°C
0.08
4-nitrophenyl benzoate
presence of 2.0 mM cetyltriphenylphosphonium bromide, pH 7.8, 27°C
0.098
4-nitrophenyl benzoate
presence of 0.5 mM cetyltriphenylphosphonium bromide, pH 7.8, 27°C
0.59
Ala-Ala-Phe-7-amido-4-methylcoumarin
pH 7.8, temperature not specified in the publication, enzyme adsorbed silica particles
1.1
Ala-Ala-Phe-7-amido-4-methylcoumarin
pH 7.8, temperature not specified in the publication, soluble enzyme
0.01
N-benzoyl-L-tyrosine 4-nitroanilide
presence of 7% dimethyl sulfoxide, pH 8.7, 25°C
0.056
N-benzoyl-L-tyrosine 4-nitroanilide
presence of 15% dimethyl sulfoxide, pH 8.7, 25°C
0.16
N-benzoyl-L-tyrosine 4-nitroanilide
water-dimethyl sulfoxide mixture encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles, 7% dimethyl sulfoxide-water, pH 8.7, 25°C
0.18
N-benzoyl-L-tyrosine 4-nitroanilide
water-dimethyl sulfoxide mixture encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles, 20% dimethyl sulfoxide-water, pH 8.7, 25°C
1.17
N-benzoyl-L-tyrosine ethyl ester
pH 8.0, 30°C, soluble enzyme
1.35 - 8.1
N-benzoyl-L-tyrosine ethyl ester
pH 8.0, 30°C, glyoxal-agarose immobilized enzymes
0.05
N-benzoyl-L-tyrosine-4-nitroanilide
presence of alpha,omega-alkanedyl-bis(hydroxyethylmethylcetyl) dibromide with a polymethylene spacer n-(CH2)10, pH 7.6, 25°C
0.07
N-benzoyl-L-tyrosine-4-nitroanilide
pH 7.6, 25°C
0.083
N-benzoyl-L-tyrosine-4-nitroanilide
presence of alpha,omega-alkanedyl-bis(hydroxyethylmethylcetyl) dibromide with a polymethylene spacer n-(CH2)6, pH 7.6, 25°C
0.024
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-4-methylpyridinium chloride, pH 7.7, temperature not specified in the publication
0.044
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-1-methylpyrrolidinium, pH 7.7, temperature not specified in the publication
0.062
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-hexyl-3-methylimidazolium chloride, pH 7.7, temperature not specified in the publication
0.065
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-3-methylimidazoliumchloride, pH 7.7, temperature not specified in the publication
0.109
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-4-methylpyridinium chloride, pH 7.7, temperature not specified in the publication
0.254
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-hexyl-3-methylimidazolium chloride, pH 7.7, temperature not specified in the publication
0.303
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-3-methylimidazoliumchloride, pH 7.7, temperature not specified in the publication
0.359
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, pH 7.7, temperature not specified in the publication
0.375
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-1-methylpyrrolidinium, pH 7.7, temperature not specified in the publication
1.05
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
10°C
3.91
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
20°C
4.37
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
50°C
4.73
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
30°C
6.79
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
40°C
0.24
N-benzoyl-L-Tyr ethyl ester
-
at 35°C
0.27
N-benzoyl-L-Tyr ethyl ester
-
at 25°C or at 10°C
0.12
N-benzoyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
3.33
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 30% methanol
6.02
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 10% methanol
2.23
N-benzoyl-L-tyrosine methyl ester
-
transesterfication in 10% ethanol
20.6
N-benzoyl-L-tyrosine methyl ester
-
transesterfication in 90% ethanol
0.11
N-benzoyl-Tyr p-nitroanilide
-
at 10°C
0.14
N-benzoyl-Tyr p-nitroanilide
-
at 25°C
0.21
N-benzoyl-Tyr p-nitroanilide
-
at 35°C
0.32
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75
0.36
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75, in the presence of 10 mM tetrabutylammonium bromide
0.94
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75, in the presence of 2.5 mM NaCl
1
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75, in the presence of 2 mM NaClO4
3.2
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75, in the presence of 1000 mM tetrabutylammonium bromide
6.1
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.75, in the presence of 400 mM tetrabutylammonium bromide
0.32
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
3
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.26
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.44
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.32
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M KCl
0.49
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 800 mM NaF
0.51
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.61
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaBr
0.92
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M LiCl
2.6
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.02
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.37
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.052
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.58
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.16
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
1.6
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.05
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
alpha-chymotrypsin, unmodified
0.07
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 2.2
0.07
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG700-alpha-chymotrypsin, degree of PEGylation: 3.8
0.08
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 1.3
0.08
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 2.9
0.08
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 4.2
0.08
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 6.0
0.09
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 4.2
0.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 1.3
0.11
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 7.6
0.15
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 8.4
0.15
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG700-alpha-chymotrypsin, degree of PEGylation: 7.9
0.19
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 9.1
0.0074
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.0087
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.5
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
0.4
N-succinyl-Ala-Phe-Ala
-
30°C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide
0.48
N-succinyl-Ala-Phe-Ala
-
30°C, pH 8.0, HPLC-based assay
0.09
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
-
at pH 6.0
0.1
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
-
at pH 4.0
0.62
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
-
at pH 6.0
0.64
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
-
at pH 4.0
0.0297
p-nitrophenyl acetate
-
in the presence of 20 mM hexadecyltrimethylammonium bromide, at 25°C
0.044
p-nitrophenyl acetate
-
at 25°C
additional information
casein
hydrolysis kinetics are analysed in the framework of a two-step model, with consecutive demasking and hydrolysis steps. Determination of kinetic parameters for casein hydrolysis by chymotrypsin using two ranges of substrate concentration
additional information
additional information
-
Michaelis-Menten metabolic rate constants (Vmax and Km) are calculated by nonlinear regression for chymotrypsin, the Vmax is 97.97 nmol/l/min and Km is 7.84 microM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
0.015
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 20, pH 7.8, 27°C
0.024
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 20, pH 7.8, 27°C
0.046
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 10, pH 7.8, 27°C
0.046
4-nitrophenyl acetate
25 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 5, pH 7.8, 27°C
0.062
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 5, pH 7.8, 27°C
0.1
4-nitrophenyl acetate
5 mM sodium 1,4-bis(2-ethylhexyl)sulfosuccinate, ratio [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 10, pH 7.8, 27°C
0.0075
4-nitrophenyl benzoate
pH 7.8, 27°C
0.0086
4-nitrophenyl benzoate
presence of 0.5 mM cetyltrimethylammonium bromide, pH 7.8, 27°C
0.013
4-nitrophenyl benzoate
presence of 2.0 mM cetyltrimethylammonium bromide, pH 7.8, 27°C
0.017
4-nitrophenyl benzoate
presence of 0.5 mM cetyltributylphosphonium bromide, pH 7.8, 27°C
0.0214
4-nitrophenyl benzoate
presence of 2.0 mM cetyltributylphosphonium bromide, pH 7.8, 27°C
0.024
4-nitrophenyl benzoate
presence of 0.5 mM cetyltriphenylphosphonium bromide, pH 7.8, 27°C
0.047
4-nitrophenyl benzoate
presence of 2.0 mM cetyltriphenylphosphonium bromide, pH 7.8, 27°C
0.45
Ala-Ala-Phe-7-amido-4-methylcoumarin
pH 7.8, temperature not specified in the publication, enzyme adsorbed silica particles
0.6
Ala-Ala-Phe-7-amido-4-methylcoumarin
pH 7.8, temperature not specified in the publication, soluble enzyme
0.013
N-benzoyl-L-tyrosine 4-nitroanilide
presence of 15% dimethyl sulfoxide, pH 8.7, 25°C
0.04
N-benzoyl-L-tyrosine 4-nitroanilide
water-dimethyl sulfoxide mixture encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles, 7% dimethyl sulfoxide-water, pH 8.7, 25°C
0.055
N-benzoyl-L-tyrosine 4-nitroanilide
water-dimethyl sulfoxide mixture encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles, 20% dimethyl sulfoxide-water, pH 8.7, 25°C
2.3
N-benzoyl-L-tyrosine 4-nitroanilide
presence of 7% dimethyl sulfoxide, pH 8.7, 25°C
0.04
N-benzoyl-L-tyrosine-4-nitroanilide
presence of alpha,omega-alkanedyl-bis(hydroxyethylmethylcetyl) dibromide with a polymethylene spacer n-(CH2)6, pH 7.6, 25°C
0.15
N-benzoyl-L-tyrosine-4-nitroanilide
pH 7.6, 25°C
0.5
N-benzoyl-L-tyrosine-4-nitroanilide
presence of alpha,omega-alkanedyl-bis(hydroxyethylmethylcetyl) dibromide with a polymethylene spacer n-(CH2)10, pH 7.6, 25°C
0.154
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-4-methylpyridinium chloride, pH 7.7, temperature not specified in the publication
0.236
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-1-methylpyrrolidinium, pH 7.7, temperature not specified in the publication
0.362
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-hexyl-3-methylimidazolium chloride, pH 7.7, temperature not specified in the publication
0.417
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.5 M 1-butyl-3-methylimidazoliumchloride, pH 7.7, temperature not specified in the publication
0.48
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-4-methylpyridinium chloride, pH 7.7, temperature not specified in the publication
0.807
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-hexyl-3-methylimidazolium chloride, pH 7.7, temperature not specified in the publication
0.985
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, pH 7.7, temperature not specified in the publication
1.054
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-3-methylimidazoliumchloride, pH 7.7, temperature not specified in the publication
1.177
N-succinyl-L-phenylalanine-4-nitroanilide
presence of 2 mM cetyltrimethylammonium bromide, 0.1 M 1-butyl-1-methylpyrrolidinium, pH 7.7, temperature not specified in the publication
0.66
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
10°C
4.13
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
20°C
8.05
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
50°C
12.8
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
30°C
21.7
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
40°C
0.56
benzoyl-D-Ala-4-guanidinophenyl ester
-
25°C, pH 7.6
6.08
benzoyl-D-Ala-4-guanidinophenyl ester
-
25°C, pH 7.6
3 - 6
benzoyl-D-Leu-4-guanidinophenyl ester
-
25°C, pH 7.6
3.04
benzoyl-D-Leu-4-guanidinophenyl ester
-
25°C, pH 7.6
1.18
benzoyl-Gly-4-guanidinophenyl ester
-
25°C, pH 7.6
6.08
benzoyl-Gly-4-guanidinophenyl ester
-
25°C, pH 7.6
130
N-acetyl-L-Tyr-ethyl ester
-
25°C, pH 7.8, in non-denaturating water-acetone oxime mixture
192
N-acetyl-L-Tyr-ethyl ester
-
25°C, pH 7.8, in non-denaturating water-1,4-butanediol mixture
205
N-acetyl-L-Tyr-ethyl ester
-
20°C, pH 8.0, in non-denaturating water-dimethylsulfoxide mixture
220
N-acetyl-L-Tyr-ethyl ester
-
20°C, pH 8.0, in non-denaturating water-ethanol mixture
0.1
N-acetyl-L-Tyr-p-nitroanilide
-
20°C, pH 8.0, in non-denaturating water-dimethylsulfoxide mixture
0.19
N-acetyl-L-Tyr-p-nitroanilide
-
20°C, pH 8.0, in non-denaturating water-ethanol mixture
119.5
N-acetyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
120
N-acetyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
43
N-benzoyl-L-Tyr ethyl ester
-
at 10°C
100
N-benzoyl-L-Tyr ethyl ester
-
at 35°C
142
N-benzoyl-L-Tyr ethyl ester
-
at 35°C
0.03 - 0.55
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 10% methanol
0.031 - 0.51
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 30% methanol
1.3
N-benzoyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
6.77
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 10% methanol
8.13
N-benzoyl-L-tyrosine ethyl ester
-
transesterfication in 30% methanol
70.4
N-benzoyl-L-tyrosine ethyl ester
-
25°C, pH 7.5
2.34
N-benzoyl-L-tyrosine methyl ester
-
transesterfication in 10% ethanol
2.94
N-benzoyl-L-tyrosine methyl ester
-
transesterfication in 10% ethanol
10.8
N-benzoyl-L-tyrosine methyl ester
-
transesterfication in 90% ethanol
0.05
N-benzoyl-Tyr p-nitroanilide
-
at pH 10°C
0.3
N-benzoyl-Tyr p-nitroanilide
-
at 25°C
0.41
N-benzoyl-Tyr p-nitroanilide
-
at 35°C
0.015
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8
0.017
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8, in the presence of 10 mM tetrabutylammonium bromide
0.025
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8, in the presence of 1000 mM tetrabutylammonium bromide
0.034
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8, in the presence of 2 mM NaClO4
0.039
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8, in the presence of 2.5 mM NaCl
0.31
N-glutaryl-L-Phe-p-nitroanilide
-
25°C, pH 7.8, in the presence of 400 mM tetrabutylammonium bromide
0.014
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.05
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.031 - 0.51
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
8.04
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
16
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.006
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.01
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M LiCl
0.026
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M KCl
0.26
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.27
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 800 mM NaF
0.34
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaBr
1.45
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
15
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
12
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
18
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.04 - 1.97
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
3.3
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
5.32
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
9.31
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
6.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG700-alpha-chymotrypsin, degree of PEGylation: 7.9
7.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 4.2
7.9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 9.1
8.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 6.0
8.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 7.6
8.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 4.2
9.4
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 8.4
10.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 2.9
10.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 2.2
11.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG700-alpha-chymotrypsin, degree of PEGylation: 3.8
12.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
alpha-chymotrypsin, unmodified
13.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG5000-alpha-chymotrypsin, degree of PEGylation: 1.3
13.5
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
PEG2000-alpha-chymotrypsin, degree of PEGylation: 1.3
77
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2, 3 M NaCl
110
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21°C, pH 8.3, 20 mM CaCl2
0.9
N-succinyl-Ala-Phe-Ala
-
30°C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide
1.2
N-succinyl-Ala-Phe-Ala
-
30°C, pH 8.0, HPLC-based assay
0.008
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
-
at pH 4.0
0.3
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
-
at pH 6.0
6.43
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester
-
at pH 6.0
0.017
p-nitrophenyl acetate
-
in 20 mM Tris/HCl pH 7.5 at 25°C
0.028
p-nitrophenyl acetate
-
in the presence of 20 mM hexadecyltrimethylammonium bromide, in 20 mM Tris/HCl pH 7.5 at 25°C
additional information
additional information
adsorption of the enzyme to silica particles leads to an 8fold increase of the turnover number
-
additional information
benzoyl-D-Phe-4-guanidinophenyl ester
-
25°C, pH 7.6
additional information
additional information
-
-
-
additional information
additional information
-
influence of dimethylsulfoxide on the turnover-number
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.344
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
-
-
0.000000027
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
-
-
0.11
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
-
0.000025
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
25°, pH 7.0
0.00057
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
25°, pH 3.2
0.019
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
at pH 7.23 and 25°C
0.024
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
at pH 7.17 and 25°C
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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
brenda
Rick, W.
Chymotrypsin
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
1045-1051
1974
Bos taurus
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Birk, Y.
A trypsin and chymotrypsin inhibitor from groundnuts (Arachis hypogaea)
Methods Enzymol.
45
716-722
1976
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Abell, A.D.; Nabbs, B.K.
Ring-deactivated hydroxymethylpyrroles as inhibitors of alpha-chymotrypsin
Bioorg. Med. Chem.
9
621-628
2001
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Yakoby, N.; Raskin, I.
A simple method to determine trypsin and chymotrypsin inhibitory activity
J. Biochem. Biophys. Methods
59
241-251
2004
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
-
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Banerjee, D.; Pal, S.K.
Conformational dynamics at the active site of alpha-chymotrypsin and enzymatic activity
Langmuir
24
8163-8168
2008
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
-
brenda
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)
brenda
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)
-
brenda
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)
-
brenda
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)
-
brenda
Verma, S.; Ghosh, K.
Effect of cationic surfactants on the enzymatic activity of alpha-chymotrypsin
Kinet. Catal.
52
6-10
2011
Bos taurus (P00766)
-
brenda
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)
brenda
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)
-
brenda
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)
brenda
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
-
brenda
Plyushchenko, A.; Borovikova, L.; Pisarev, O.
Proteolytic activity of chymotrypsin immobilized on selenium nanoparticles
Appl. Biochem. Microbiol.
54
375-378
2018
Bos taurus (P00766)
-
brenda
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)
brenda
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)
brenda
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)
brenda
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)
-
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
-
brenda
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)
-
brenda
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)
-
brenda