Information on EC 3.4.21.1 - chymotrypsin

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The expected taxonomic range for this enzyme is: Tenebrio molitor

EC NUMBER
COMMENTARY
3.4.21.1
-
RECOMMENDED NAME
GeneOntology No.
chymotrypsin
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage: Tyr-/-, Trp-/-, Phe-/-, Leu-/-
show the reaction diagram
-
-
-
-
Preferential cleavage: Tyr-/-, Trp-/-, Phe-/-, Leu-/-
show the reaction diagram
specific cleavage of the Phe18-Asp19 peptide bond in the trypsinogen activation peptide and removal of the N-terminal tripeptide
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4CHA
-
-
Alcalase
-
-
alpha chymar
-
-
-
-
alpha chymotrypsin
-
-
alpha-chymar ophth
-
-
-
-
alpha-chymotrypsin
-
-
-
-
alpha-chymotrypsin
-
type I-S
alpha-chymotrypsin
P00766
part of the chymotrypsin-BTCI-trypsin ternary complex
alpha-chymotrypsin
-
-
alpha-chymotrypsin
-
-
alpha-chymotrypsin
-
-
alpha-chymotrypsin
-
-
alpha-chymotrypsin
-
-
alpha-chymotrypsin A
-
-
-
-
avazyme
-
-
-
-
bovine alpha-chymotrypsin
-
-
caldecrin
-
-
cationic chymotrypsin
-
-
cellulomonadin
-
-
Chtp
-
-
ChTRP
-
-
chymar
-
-
-
-
chymotest
-
-
-
-
chymotrypsin
-
-
chymotrypsin
-
-
chymotrypsin
Q1M0X9
-
chymotrypsin
Q86M89
-
chymotrypsin
-
-
chymotrypsin
-
-
chymotrypsin A
-
-
-
-
chymotrypsin A
-
anionic chymotrypsin
chymotrypsin B
-
-
-
-
chymotrypsin B
-
cationic chymotrypsin
chymotrypsin B
P07338
-
chymotrypsin C
-
-
chymotrypsin C1
-
-
chymotrypsin I
-
-
chymotrypsin II
-
-
chymotrypsin isoform Kh1
-
-
chymotrypsin isoform Kh2
-
-
chymotrypsin isoform Kh3
-
-
chymotrypsin-B
-
-
CTRA
-
-
Ctrb
P07338
-
E.C. 3.4.4.5
-
-
-
-
E.C. 3.4.4.6
-
-
-
-
enzeon
-
-
-
-
LBCP
P07338
-
lysosomal Bid cleavage protease
P07338
-
PEG-alpha-chymotrypsin
-
-
PEG-modified alpha-chymotrypsin
-
-
quimar
-
-
-
-
quimotrase
-
-
-
-
serine protease
-
-
CAS REGISTRY NUMBER
COMMENTARY
9004-07-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
alpha chymotrypsin A
UniProt
Manually annotated by BRENDA team
alpha-chymotrypsin
-
-
Manually annotated by BRENDA team
Diabrotica virgifera virgifera
-
-
Manually annotated by BRENDA team
2 enzyme forms: A and B
-
-
Manually annotated by BRENDA team
2 enzyme forms: LCTa and LCTb
-
-
Manually annotated by BRENDA team
isoenzyme CTRA-1
-
-
Manually annotated by BRENDA team
Sardinops sagax caerulea, Monterey sardine
-
-
Manually annotated by BRENDA team
European catfish
-
-
Manually annotated by BRENDA team
fire ant
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
anti-chymotrypsin B weakly cross reacts with chymotrypsin A
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]ethanaminium + H2O
?
show the reaction diagram
-
-
-
-
?
4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
4-[2-(2-[[4-([1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]amino)-4-oxobutanoyl]amino]ethoxy)ethoxy]butanoate + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Tyr ethyl ester + H2O
acetyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
acetyl-Leu methyl ester + H2O
acetyl-Leu + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Phe ethyl ester + H2O
acetyl-Phe + ethanol
show the reaction diagram
-
-
-
-
?
acetyl-Trp ethyl ester + H2O
acetyl-Trp + ethanol
show the reaction diagram
-
-
-
-
?
acetyl-Tyr ethyl ester + H2O
acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
?
benzoyl-4-guanidinophenyl ester + H2O
benzoyl + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-D-Ala-4-guanidinophenyl ester + H2O
benzoyl-D-Ala + 4-guanidinophenol
show the reaction diagram
-
5% of activity with N-benzoyl-L-Ala-4-guanidinophenyl ester
-
?
benzoyl-D-Leu-4-guanidinophenyl ester + H2O
benzoyl-D-Leu + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-D-Phe-4-guanidinophenyl ester + H2O
benzoyl-D-Phe + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-Gly-4-guanidinophenyl ester + H2O
benzoyl-Gly + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-L-Ala-4-guanidinophenyl ester + H2O
benzoyl-L-Ala + 4-guanidinophenol
show the reaction diagram
-
-
-
?
benzoyl-L-tyrosine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-L-tyrosine ethyl ester + H2O
benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-Tyr-p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-tyrosine p-nitroanilide + H2O
benzoyl-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
beta-lactoglobulin A + H2O
?
show the reaction diagram
-
-
chymotrypsin hydrolyzes beta-lactoglobulin A after Tyr, Trp, Phe, Met, and Leu, peptides corresponding to the cleavage of bonds with Glu, Gln, and Lys at the N-terminal side are also found
-
?
BH3 interacting domain death agonist + H2O
?
show the reaction diagram
P07338
-
-
-
?
bovine chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
bovine serum albumine + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
Q7SIG2
-
-
?
cationic trypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
cheese whey protein + H2O
?
show the reaction diagram
-
-
-
-
r
deltamethrin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
chymotrypsin A is active in degrading gelatin, while chymotrypsin B does not reveal activity against gelatin
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
1 mM in 25mM Tris-HCl buffer containing 0.5M NaCl
-
-
?
L-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Tyr ethyl ester + H2O
L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
L-Tyr ethyl ester + H2O
L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
m-calpain + H2O
fragments of m-calpain
show the reaction diagram
-
-
-
?
mCry3A + H2O
mCry3A fragments
show the reaction diagram
-
Bacillus thuringiensis toxin
chymotrypsin cleaves mCry3A into stable 55000 and 49000 Da fragments, as well as smaller polypeptides having molecular masses of 6000 to 11000 Da
-
?
mu-calpain + H2O
fragments of mu-calpain
show the reaction diagram
-
-
-
?
N-acetyl-DL-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-DL-Phe-beta-naphthylester + H2O
N-acetyl-DL-Phe + beta-naphthol
show the reaction diagram
-
-
-
?
N-acetyl-DL-phenylglycine methyl ester + H2O
N-acetyl-L-phenylglycine + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
enatiomeric excess greater than 99%
?
N-acetyl-L-leucine methyl ester + H2O
N-acetyl-L-leucine + methanol
show the reaction diagram
-
5% of kcat with N-acetyl-L-tyrosine ethyl ester
-
?
N-acetyl-L-Phe methyl ester + H2O
N-acetyl-L-Phe + methanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
-
?
N-acetyl-L-Phe-Ala-Thr-Pal-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Pal + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-CN) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOH)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOH) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-COOMe) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-guanidine) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NH2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe-(p-NO2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Phe-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Phe + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid + H2O
N-acetyl-L-Phe-Ala-Thr-Tyr + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + glycinamide
N-Ac-Phe-Gly-NH2 + ethanol
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + H2O
N-acetyl-L-phenylalanine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-tryptophan ethyl ester + H2O
N-acetyl-L-tryptophan + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr-ethyl ester + H2O
N-acetyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-Tyr-p-nitroanilide + H2O
N-acetyl-L-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine
show the reaction diagram
-
-
-
?
N-alpha-acetyl-L-tyrosine ethyl ester + H2O
N-alpha-acetyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
? + p-nitroaniline
show the reaction diagram
-
BApNA
-
-
?
N-alpha-benzoyl-L-tyrosine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-tyrosyl ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-arginine ethyl ester + H2O
N-benzoyl-L-arginine + ethanol
show the reaction diagram
-
0.5 mM in 50 mM phosphate buffer, pH 7.6
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
-
alpha-chymotrypsin immobilized to mesoporous silica
-
?
N-benzoyl-L-Tyr p-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
show the reaction diagram
Q1M0X9
-
-
-
?
N-benzoyl-L-Tyr-p-nitroanilide + H2O
N-benzoyl-tyrosine + 4-nitroaniline
show the reaction diagram
Q86M89, -
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + methanol
N-benzoyl-L-tyrosine methyl ester + ethanol
show the reaction diagram
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + ethanol
N-benzoyl-L-tyrosine ethyl ester + methanol
show the reaction diagram
-
transesteriferication
-
?
N-benzoyl-L-tyrosine methyl ester + H2O
N-benzoyl-L-tyrosine + methanol
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-Tyr p-nitroanilide + H2O
N-benzoyl-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2)-5-amido-2-nitrobenzoic acid + H2O
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Phe-(p-NO2) + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr-5-amido-2-nitrobenzoic acid + H2O
N-benzyloxycarbonyl-L-Phe-Ala-Thr-Tyr + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
N-glutamyl-L-phenylalanine p-nitroanilide + H2O
p-nitroaniline + N-glutamyl-L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-glutaryl-L-Phe-p-nitroanilide + H2O
N-glutaryl-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-glutaryl-L-phenylalanine-p-nitroanilide + H2O
N-glutaryl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Ala p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
Q1M0X9
-
-
-
?
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
Q86M89, -
-
-
-
?
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Arg + p-nitroaniline
show the reaction diagram
-
very low activity
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Pro-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Lys + p-nitroaniline
show the reaction diagram
-
extremly low activity
-
?
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nle + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Nva + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
preferred substrate
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
P00766
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
SucAAPFpNA
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
Q1M0X9
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
Q86M89, -
-
-
-
?
N-succinyl-Ala-Phe-Ala + H2O
N-succinyl-Ala-Phe + alanine
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Ala-Ala-Pro-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-L-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine p-nitroanilide + H2O
p-nitroaniline + N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-p-nitroanilide + H2O
p-nitroaniline + N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Phe-p-nitroanilide + H2O
N-succinyl-L-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-phenylalanine p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-phenylalanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Q1M0X9
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Q86M89, -
-
-
-
?
N-succinyl-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
Q1M0X9
-
-
-
?
N-succinyl-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
Q86M89, -
-
-
-
?
N-succinyl-Phe-p-nitroanilide + H2O
p-nitroaniline + N-succinyl-Phe
show the reaction diagram
-
-
-
-
?
N-[1-benzyl-2-[(4-nitrophenyl)amino]-2-oxoethyl]-N'-[2-[2-(2-hydroxyethoxy)ethoxy]ethyl]butanediamide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Ala p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Ala + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Leu p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Leu + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Tyr + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-L-Tyr benzyl ester + H2O
Nalpha-tosyl-L-Tyr + phenol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
catalyzes the hydrolysis of peptide bonds of protein foods in mammalian gut
-
-
-
Protein + H2O
?
show the reaction diagram
-
enzyme form LCTb plays an important role in establishing the myiasis-causing larvae of Lucilia cuprina on host skin as well as providing nutrients for the rapidly growing larvae
-
-
-
rat chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
SPPNA + H2O
?
show the reaction diagram
-
specific substrate for chymotrypsin
-
-
?
succinimidyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinimidyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
-, Q9Y843
42% of activity with succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
?
succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Met + p-nitroaniline
show the reaction diagram
-, Q9Y843
66% of activity with succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
57 microM, pH 7.8
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-, Q9Y843
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Gly-p-nitroanilide + H2O
succinyl-Gly-Gly + p-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide + H2O
succinyl-L-Ala-Ala-Pro-L-phenylalanine + p-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
chymotrypsin A shows much lower catalytic efficiency to the substrate than chymotrypsin B
-
-
?
Trypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-Thr-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Z-Phe-Arg-Thr-Tyr + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
milk-acetate mixture + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
specific hydrolysis of peptide bonds on the carboxyl side of Tyr, Phe, Trp, His, Leu Thr and Gly
-
-
-
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
?
-
-
does not cleave the Bacillus thuringiensis toxin Cry3A
-
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bovine chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
catalyzes the hydrolysis of peptide bonds of protein foods in mammalian gut
-
-
-
Protein + H2O
?
show the reaction diagram
-
enzyme form LCTb plays an important role in establishing the myiasis-causing larvae of Lucilia cuprina on host skin as well as providing nutrients for the rapidly growing larvae
-
-
-
rat chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Trypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
5 mM, 1.5fold increase in activity, destabilizes the enzyme-pancreatic trypsin inhibitor complex formation
Ca2+
-
required for catalysis
Ca2+
-
both chymotrypsin A and B are slightly activated at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 115% and 103% relative activity for chymotrypsin A and B, respectively
Ca2+
-
required for catalysis
Mg2+
-
both chymotrypsin A and B are slightly activated at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 111% and 110% relative activity for chymotrypsin A and B, respectively
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(Cbz-alanyl)aminomethyl boronic acid
-
inhibition decreases in the presence of arabinogalactan
(Cbz-phenylalanyl)aminomethyl boronic acid
-
inhibition decreases in the presence of arabinogalctan
(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium (V)
-
-
(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
-
-
(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-mercaptoethanol
-
-
2-nitrophenyl-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
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
3,4-Dichloroisocoumarin
P07338
complete inhibition at 0.2 mM
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
-
-
4-[(4-nitrophenyl)sulfonyl]-1,2,7,8-tetradehydro-3,4,5,6-tetrahydro-4-benzazecine
-
-
5'-demethoxyepiexcelsin
-
from Commiphora mukul, noncompetitive inhibitor
-
7-hydroxycoumarin
-
0.78 mM, 50% inhibition
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 confusa chymotrypsin inhibitor
-
large, dimeric 70 kDa chymotrypsin inhibitor with a molar ratio of inhibition between the chymotrypsin inhibitor and alpha-chymotrypsin of 2:1, which gives about 100% inhibition. The molar ratio of chymotrypsin inhibitor to chymotrypsin is usually 1:1. Its chymotrypsin inhibitory activity is stable from pH 3-10 and from 0-50C. Exerts antiproliferative activity toward breast cancer MCF-7 cells
-
Acacia plumosa trypsin inhibitor A
-
strong inhibition
-
Acacia plumosa trypsin inhibitor B
-
strong inhibition
-
Acacia plumosa trypsin inhibitor C
-
strong inhibition
-
aceto[2,6-bis[(butylthio-jS)methyl]phenyl-kappaC]-,(SP-4-3)-palladium(II)
-
-
alpha-chymostatin
-
specific inhibitor
alpha1-Antichymotrypsin
-
forms very long-lived, enzymatically inactive 1/1 compexes with its target
-
alpha2-Macroglobulin
-
nonspecific proteinase inhibitor
-
Alzheimer's amyloid beta-protein precursor
-
engineering of inhibitors with altered specificities
-
anti-trypsin-chymotrypsin A
-
highly potent serine protease inhibitor protein from Theromyzon tessulatum
-
anti-trypsin-chymotrypsin B
-
highly potent serine protease inhibitor protein from Theromyzon tessulatum
-
Aprotinin
P07338
partial inhibition at 0.1 mg/ml
AVPGSWPW
-
octapeptide
basic pancreatic trypsin inhibitor
-
engineering of inhibitors with altered specificities
-
basic pancreatic trypsin inhibitor
-
-
-
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
-
Belactosin C
-
irreversible inhibitor
Benzamidine
-
-
Benzamidine
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, inhibits chymotrypsin II, whereas chymotrypsin I is not inhibited
Benzamidine
-
partially inhibits both chymotrypsin A and B. At room temperature, at 5 mM concentration, 60.3% and 62.5% residual activity for chymotrypsin A and B, respectively
benzyloxycarbonyl-Ala-Ala-Phe-glyoxal
-
-
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
extremely potent inhibitor
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
-
-
black-eyed pea trypsin/chymotrypsin inhibitor
P00766
BTCI, is able to inhibit trypsin and chymotrypsin simultaneously by forming a stable ternary complex
-
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
-
-
BPTI
-
basic pancreatic trypsin inhibitor, inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8. With 0.5 M NaCl no inhibition detected
-
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
-
Cd2+
-
partially inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 76.8% and 49.7% residual activity for chymotrypsin A and B, respectively
chicken ovomucoid inhibitor
-
-
-
chloro[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
-
-
chymostatin
-
-
chymostatin
-
-
chymostatin
-
-
chymostatin
-
strong inhibitory effect in concentrations starting from 0.001 mM, 50% inhibition by 0.05 mM
chymostatin
P07338
complete inhibition at 0.25 mM
chymostatin
-
effectively inhibits both chymotrypsin A and B. At room temperature, at 0.01 mM concentration, no residual activity for both chymotrypsin A and B
CMTI I
-
Cucurbita maxima trypsin inhibitor, unusual interaction with the highly selective protein trypsin inhibitor from Cucurbita maxima, inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8, with 0.5 M NaCl increased inhibitory effect
-
CMTI IV
-
Cucurbita maxima trypsin inhibitor, unusual interaction with the highly selective protein trypsin inhibitor from Cucurbita maxima, inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8, with 0.5 M NaCl increased inhibitory effect
-
complex of vanadate and benzohydroxamic acid
-
competitive inhibitor of alpha-chymotrypsin, consisting of 1 mM vanadate and 2 mM benzohydroxamic acid
CPGT I
-
Cucurbita pepo var. giramontia inhibitor, Chtr1 in 0.1 M Tris-HCl, pH 7.8: no inhibition. With 0.5 M NaCl inhibition observed
-
CPTI IV
-
Cucurbita pepo inhibitor, Chtr1 in 0.1 M Tris-HCl, pH 7.8: no inhibition. With 0.5 M NaCl inhibition observed
-
Cu2+
-
strongly inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 0% and 2.5% residual activity for chymotrypsin A and B, respectively
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
CyPTI VII
-
trypsin inhibitors from Cyclanthera pedata, Chtr1 in 0.1 M Tris-HCl, pH 7.8: no inhibition. With 0.5 M NaCl inhibition observed
-
dammara-20,24-dien-3beta-ol
-
0.00013 mM, 50% inhibition, competitive inhibition
diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
EDTA
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, inhibits chymotrypsin II, whereas chymotrypsin I is not inhibited
EDTA
-
shows minimal inhibitory effect on both chymotrypsin A and B. At room temperature, at 1 mM concentration, 99% and 97% residual activity for chymotrypsin A and B, respectively
Eglin c
-
-
epiexcelsin
-
from Commiphora mukul, noncompetitive inhibitor
-
faradiol 3-O-myristate
-
0.000032 mM, 50% inhibition, noncompetitive inhibition
faradiol 3-O-palmitate
-
0.000072 mM, 50% inhibition, noncompetitive inhibition
Fe2+
-
strongly inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 14.6% and 21.1% residual activity for chymotrypsin A and B, respectively
-
GAW
-
tripeptide
Gly-Arg-cyclo[-S-Cys-Thr-Pal-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-CH3)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-F)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-guanidine)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-NH2)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Phe(p-NO2)-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
Gly-Arg-cyclo[-S-Cys-Thr-Tyr-Ser-Ile-Pro-Pro-Ile-Cys-S-]-Phe-Pro-Asp
-
-
IVNGEEAVPGSWPW
-
autocatalytically produced 14-residue fragment from a three-phase-partitioning-treated chymotrypsin
Leu-Phe-p-fluorophenylmethylamide
-
strong inhibition
lima bean inhibitor
-
-
-
lima bean inhibitor
-
-
-
lima bean trypsin inhibitior
-
-
-
lup-20(29)-ene-3beta,16beta-diol
-
0.00012 mM, 50% inhibition, competitive inhibition
LUTI
-
Linum usitatissimum inhibitor, inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8, with 0.5 M NaCl increased inhibitory effect
-
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
MG-132
-
reversible inhibitor
micropeptin 478-A
-
potent inhibitor
micropeptin 478-B
-
moderate inhibitor
micropeptin HU1021
-
weak inhibitor
micropeptin HU1041
-
weak inhibitor
micropeptin HU1069
-
weak inhibitor
micropeptin HU895A
-
moderate inhibitor
micropeptin HU895B
-
potent inhibitor
micropeptin HU909
-
potent inhibitor
micropeptin HU975
-
moderate inhibitor
micropeptin HU989
-
moderate inhibitor
mixed monolayer protected gold cluster
-
anionically functionalized amphiphilic nanoparticles
-
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
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
irreversible inhibitor
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
irreversible inhibitor
N-(tert-butoxycarbonyl)-L-leucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
irreversible inhibitor
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
irreversible inhibitor
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-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
irreversible inhibitor, significant inhibition of 20S proteasome chymotrypsin-like (beta5) activity, inhibitory potency is similar to that of Belactosin C
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
irreversible inhibitor, possesses the greatest inhibition of the chymotrypsin-like activity, inhibitory potency is similar to that of Belactosin C. Increases the G2/M cell distribution in a similar manner to that of PS-341, and induces apoptosis at more than 0.001 mM concentration of compound in HeLa cells
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
irreversible 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-alpha-tosyl-L-Phe chloromethyl ketone
Q1M0X9
TPCK
N-alpha-tosyl-L-Phe chloromethyl ketone
Q86M89, -
TPCK
N-alpha-tosyl-L-Phe chloromethyl ketone
-
TPCK
N-benzoyl-L-tyrosine ethyl ester
-
-
N-carbobenzoxy-Gly-Gly-Phe-chloromethyl ketone
-
Z-GGF-CK
N-carbobenzoxy-Gly-Gly-Phe-chloromethyl ketone
Q1M0X9
Z-GGF-CK
N-carbobenzoxy-Gly-Gly-Phe-chloromethyl ketone
Q86M89, -
Z-GGF-CK
N-carbobenzoxy-Gly-Gly-Phe-chloromethyl ketone
-
Z-GGF-CK
N-p-tosyl-L-phenylalanine-chloromethyl ketone
P07338
complete inhibition at 5 mM
N-succinyl-L-phenylalanine
-
-
N-toluenesulfonyl-L-phenylalanine chloromethyl-ketone
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, partially inhibits (53% residual activity)
N-toluenesulfonyl-L-phenylalanine chloromethylketone
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, partially inhibits chymotrypsin I (56% residual activity) and chymotrypsin II (60% residual activity)
N-toluenesulfonyl-L-phenylalanine-chloromethyl ketone
-
56% residual activity at 1 mg/ml
N-tosyl-L-Phe-Ala-Thr-Phe-(p-NO2) aldehyde
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
significant inhibition, especially to chymotrypsin B. At room temperature, at 0.05 mM concentration, 35.6% and 17.5% residual activity for chymotrypsin A and B, respectively
N-tosyl-L-phenylalanine-chloromethyl ketone
-
chymotrypsin inhibitor TPCK
N2-(tert-butoxycarbonyl)-N4-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-aspartamide
-
irreversible inhibitor
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
irreversible inhibitor
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
irreversible inhibitor
p-nitrophenyl-p'-guanidino-benzoate
-
NPGB
p-octyloxybenzyltributylammonium bromide
-
5 mM, approx. 90% inactivation after 24 h
p-octyloxybenzyltrimethylammonium bromide
-
10 mM, complete inactivation
p-tosyl-L-phenylalanine chloromethane
-
-
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
-
Pefabloc SC
-
effectively inhibits both chymotrypsin A and B. At room temperature, at 1 mM concentration, 1.2% and 1.1% residual activity for chymotrypsin A and B, respectively
Pepstatin
-
shows minimal inhibitory effect on both chymotrypsin A and B. At room temperature, at 0.03 mM concentration, 95.9% and 92.3% residual activity for chymotrypsin A and B, respectively
Phenylboronic acid
-
-
phenylmethanesulfonyl fluoride
-
effectively inhibits both chymotrypsin A and B. At room temperature, at 1 mM concentration, 0.4% and 0.3% residual activity for chymotrypsin A and B, respectively
phenylmethylsulfonyl fluoride
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits chymotrypsin I and chymotrypsin II (1-2% residual activity)
phenylmethylsulfonyl-fluoride
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits (4% residual activity)
Phenylmethylsulfonylfluoride
Q7SIG2
-
Phenylmethylsulfonylfluoride
-
the enzymatic activity is completely lost at 1 mM and room temperature
Phenylmethylsulfonylfluoride
-
1% residual activity at 1.4 mg/ml
Phenylmethylsulfonylfluoride
P07338
complete inhibition at 2 mM
photolytic 1-(2-nitrophenyl)ethanol residues
-
1-(2-nitrophenyl)ethanol coated protein can be reactivated by 15 min UV-A radiation
-
Proflavin
-
-
Proflavin
-
substrate mimic inhibitor
PS-341
-
reversible inhibitor
S-(3'-chlorophenyl)-6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carbothioate
-
-
SERPINB3
P07338
partial inhibition
-
SERPINB4
P07338
partial inhibition
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
6% residual activity at 0.5 mg/ml
-
Soybean trypsin inhibitor
P07338
complete inhibition at 0.1 mg/ml
-
Soybean trypsin inhibitor
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits (17% residual activity)
-
Soybean trypsin inhibitor
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, fully inhibits chymotrypsin I and chymotrypsin II (no residual activity)
-
STI
-
soybean trypsin inhibitor, inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8. With 0.5 M NaCl no inhibition detected
-
Suc-Val-Pro-PheP(OPh)2
-
most potent phosphonate chymotrypsin inhibitor
symplocamide A
-
from the Marine Cyanobacterium Symploca sp.. A potent cancer cell cytotoxin, which also inhibits serine proteases with a 200fold greater inhibition of chymotrypsin over trypsin
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
-
-
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
tirucalla-7,24-dien-3beta-ol
-
0.000098 mM, 50% inhibition, noncompetitive inhibition
tosyl-L-phenylalanine chloromethyl ketone
-
TPCK. Inhibition of Chtr1 in 0.1 M Tris-HCl, pH 7.8. With 0.5 M NaCl no inhibition detected
TPGVY
-
pentapeptide
trypsin inhibitor I-S
-
from soybean
-
trypsin-inhibitor
-
from Glycine max cv. Small Glossy Black
-
turkey ovomucoid inhibitor
-
-
-
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
Mn2+
-
partially inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 85.3% and 48.9% residual activity for chymotrypsin A and B, respectively
additional information
-
an inhibitor from Arachis hypogaea
-
additional information
-
no inhibition by N-p-tosyl-lysine chloroketone and 4-(amidinopheyl)methanesulfonyl fluoride
-
additional information
-
not inhibited by 0.25 mg/ml EDTA or 2 mg/ml benzamidine
-
additional information
P07338
not inhibited by benzamide and L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
additional information
-
not inhibited by 4',6-diamidino-2-phenylindole
-
additional information
-
affinity of Chtr1 to inhibitors containing Arg at P1 position. N-alpha-tosyl-L-lysine chloromethyl ketone (TLCK), Chtr1 in 0.1 M Tris-HCl, pH 7.8: no inhibition
-
additional information
-
overview about structure-activity relationships for all Ahp-containing depsipeptides with inhibitory activity against trypsin or chymotrypsin
-
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
-
boron peptides selectively inhibit the chymotrypsin-like activity (beta5) of 20S proteasome
-
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
-
efficient binding and inhibition of ChT by a self-assembled DNA quadruplex with protein recognition fragments appended on the 5'-ends of the assembled G-quartet: quadruplex containing two anionic residues in each loop (GDGD) displays the highest inhibition potency for ChT, exhibits slow binding inhibition. Quadruplex containing one anionic and one hydrophobic residue (GDGY) strongly inhibits ChT activity, exhibits slow binding inhibition. Quadruplex without tethered loops or containing a peptide loop tethered to a single strand of a sequence that is incapable of forming self-assembled structures, are weak inhibitors
-
additional information
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, is not inhibited by benzamidine and EDTA
-
additional information
-
substitution of the phosphonate diphenyl ester rings by a variety of different substituents at different positions does not significantly improve inhibitory activity
-
additional information
-
lowest inhibition concentrations of chymotrypsin for glyceric acid at position 7, while 3-sulfoglyceric acid derivatives are less potent and disulfoglyceric acid derivatives exert much higher IC50's
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cetyltributylammonium bromide
-
promotes activity
dodecyltrimethylammonium bromide
-
2-20 mM
p-octyloxybenzyltributylammonium bromide
-
maximal activation at 5 mM, inhibition at extended incubation
tetrabutylammonium bromide
-
400 mM, approx. 4fold activation
tetrabutylammonium bromide
-
promotes activity
tetrapentylammonium bromide
-
-
Trypsin
-
-
-
Hexadecyltrimethylammonium bromide
-
2-60 mM, aqueous micelles of the cationic polymeric surfactant hexadecyltrimethylammonium bromide
additional information
-
15 min UV-A radiation reactivates 1-(2-nitrophenyl)ethanol coated enzyme
-
additional information
-
not affected by putrescine or spermidine
-
additional information
-
during purification, both chymotrypsin A and B are fully activated when extracted
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
acetyl-Leu methyl ester
-
-
7.27
-
acetyl-Leu methyl ester
-
-
1.04
-
acetyl-Phe ethyl ester
-
-
1.39
-
acetyl-Phe ethyl ester
-
-
0.17
-
acetyl-Trp ethyl ester
-
-
1.12
-
acetyl-Trp ethyl ester
-
-
1.27
-
Acetyl-Tyr ethyl ester
-
-
2
-
Acetyl-Tyr ethyl ester
-
-
1.05
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
10C
3.91
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
20C
4.37
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
50C
4.73
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
30C
6.79
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
40C
0.44
-
benzoyl-4-guanidinophenyl ester
-
25C, pH 7.6
4.94
-
benzoyl-D-Ala-4-guanidinophenyl ester
-
25C, pH 7.6
1.49
-
benzoyl-D-Leu-4-guanidinophenyl ester
-
25C, pH 7.6
2.58
-
benzoyl-D-Phe-4-guanidinophenyl ester
-
25C, pH 7.6
2.81
-
benzoyl-Gly-4-guanidinophenyl ester
-
25C, pH 7.6
2.88
-
benzoyl-L-Ala-4-guanidinophenyl ester
-
25C, pH 7.6
0.13
-
benzoyl-Tyr ethyl ester
-
-
7.02
-
N-acetyl-L-leucine methyl ester
-
25C, pH 7.5
8.72
-
N-acetyl-L-leucine methyl ester
-
25C, 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
-
25C, pH 7.5
2.58
-
N-acetyl-L-phenylalanine ethyl ester
-
25C, pH 7.5
0.14
-
N-acetyl-L-tryptophan ethyl ester
-
25C, pH 7.5
0.19
-
N-acetyl-L-tryptophan ethyl ester
-
25C, pH 7.5
0.57
-
N-Acetyl-L-tyrosine ethyl ester
-
25C, pH 7.5
1.17
-
N-Acetyl-L-tyrosine ethyl ester
-
25C, pH 7.5
0.939
-
N-alpha-benzoyl-DL-arginine-p-nitroanilide
-
-
0.1
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form B, at 35C
-
0.12
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 10C
-
0.14
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 25C
-
0.17
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 35C
-
0.2
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form B, at 25C or 10C
-
0.24
-
N-benzoyl-L-Tyr ethyl ester
-
at 35C
-
0.27
-
N-benzoyl-L-Tyr ethyl ester
-
at 25C or at 10C
-
0.12
-
N-benzoyl-L-tyrosine ethyl ester
-
25C, pH 7.5
0.13
-
N-benzoyl-L-tyrosine ethyl ester
-
25C, 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
0.08
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A and enzyme form B, at 25C
0.09
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A, at 10C
0.11
-
N-benzoyl-Tyr p-nitroanilide
-
at 10C
0.11
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form B, at 10C; enzyme form B, at 35C
0.14
-
N-benzoyl-Tyr p-nitroanilide
-
at 25C
0.14
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A, at 35C
0.21
-
N-benzoyl-Tyr p-nitroanilide
-
at 35C
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
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75
0.36
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75, in the presence of 10 mM tetrabutylammonium bromide
0.94
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75, in the presence of 2.5 mM NaCl
1
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75, in the presence of 2 mM NaClO4
3.2
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75, in the presence of 1000 mM tetrabutylammonium bromide
6.1
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.75, in the presence of 400 mM tetrabutylammonium bromide
0.0013
-
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
0.006
-
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
Q1M0X9
-
0.01
-
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
0.013
-
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
0.023
-
N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
Q86M89, -
-
0.32
-
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
3
-
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.26
-
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.44
-
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.32
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M KCl
0.49
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 800 mM NaF
0.51
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.61
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaBr
0.92
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M LiCl
2.6
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.02
-
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.37
-
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.052
-
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.58
-
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.16
-
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
1.6
-
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, 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; 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; PEG5000-alpha-chymotrypsin, degree of PEGylation: 2.9; PEG5000-alpha-chymotrypsin, degree of PEGylation: 4.2; 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; 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
-
21C, pH 8.3, 20 mM CaCl2
0.0087
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.02
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
chymotrypsin 4
0.2
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
Q86M89, -
-
0.3
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
0.5
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
1.1
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
Q1M0X9
-
0.4
-
N-succinyl-Ala-Phe-Ala
-
30C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide
0.48
-
N-succinyl-Ala-Phe-Ala
-
30C, pH 8.0, HPLC-based assay
2.5
-
N-succinyl-Ala-Phe-p-nitroanilide
-
30C, pH 8.0
0.044
-
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide
-
at 25C
0.074
-
N-succinyl-L-Ala-Ala-Pro-p-nitroanilide
-
in 50 mM Tris-HCl pH 8.0 with 10 mM CaCl2, at 30 C
0.14
-
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 25C
1.09
-
N-succinyl-L-Phe-p-nitroanilide
-
at 25C
0.01
-
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin
Q1M0X9
-
0.022
-
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
-
0.025
-
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin
Q86M89, -
-
0.032
-
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
-
2.3
-
N-succinyl-Phe-7-amido-4-methylcoumarin
-
-
2.4
-
N-succinyl-Phe-7-amido-4-methylcoumarin
Q86M89, -
-
3
-
N-succinyl-Phe-7-amido-4-methylcoumarin
-
-
5
-
N-succinyl-Phe-7-amido-4-methylcoumarin
Q1M0X9
-
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
0.08
-
Nalpha-benzyloxycarbonyl-L-Tyr p-nitrophenyl ester
-
-
0.4
-
Nalpha-tosyl-L-Tyr benzyl ester
-
-
0.0297
-
p-nitrophenyl acetate
-
in the presence of 20 mM hexadecyltrimethylammonium bromide, at 25C
0.044
-
p-nitrophenyl acetate
-
at 25C
0.022
-
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
37C, pH 8.0
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
0.048
-
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 30C, chymotrypsin II
0.074
-
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 30C, chymotrypsin I
0.012
-
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
-
37C, pH 8.0
0.09
-
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30C
0.0005
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin B, at pH 7.5 and 37C
0.0014
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin A, at pH 7.5 and 37C
0.8
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37C
0.64
-
benzoyl-Tyr ethyl ester
-
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.6
-
acetyl-Leu methyl ester
-
-
22.1
-
acetyl-Leu methyl ester
-
-
5.3
-
acetyl-Phe ethyl ester
-
-
52.4
-
acetyl-Phe ethyl ester
-
-
9.3
-
acetyl-Trp ethyl ester
-
-
48.4
-
acetyl-Trp ethyl ester
-
-
25.4
-
Acetyl-Tyr ethyl ester
-
-
126
-
Acetyl-Tyr ethyl ester
-
-
0.66
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
10C
4.13
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
20C
8.05
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
50C
12.8
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
30C
21.7
-
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
40C
0.13
-
benzoyl-4-guanidinophenyl ester
-
25C, pH 7.6
0.56
-
benzoyl-D-Ala-4-guanidinophenyl ester
-
25C, pH 7.6
6.08
-
benzoyl-D-Ala-4-guanidinophenyl ester
-
25C, pH 7.6
3
6
benzoyl-D-Leu-4-guanidinophenyl ester
-
25C, pH 7.6
5.54
-
benzoyl-D-Phe-4-guanidinophenyl ester
-
25C, pH 7.6
1.18
-
benzoyl-Gly-4-guanidinophenyl ester
-
25C, pH 7.6
6.08
-
benzoyl-Gly-4-guanidinophenyl ester
-
25C, pH 7.6
10.4
-
benzoyl-L-Ala-4-guanidinophenyl ester
-
25C, pH 7.6
57.5
-
benzoyl-Tyr ethyl ester
-
-
4.6
-
N-acetyl-L-leucine methyl ester
-
25C, pH 7.5
6.5
-
N-acetyl-L-leucine methyl ester
-
25C, 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
-
-
40.3
-
N-acetyl-L-phenylalanine ethyl ester
-
25C, pH 7.5
54.8
-
N-acetyl-L-phenylalanine ethyl ester
-
25C, pH 7.5
25.7
-
N-acetyl-L-tryptophan ethyl ester
-
25C, pH 7.5
48.8
-
N-acetyl-L-tryptophan ethyl ester
-
25C, pH 7.5
130
-
N-acetyl-L-Tyr-ethyl ester
-
25C, pH 7.8, in non-denaturating water-acetone oxime mixture
192
-
N-acetyl-L-Tyr-ethyl ester
-
25C, pH 7.8, in non-denaturating water-1,4-butanediol mixture
205
-
N-acetyl-L-Tyr-ethyl ester
-
20C, pH 8.0, in non-denaturating water-dimethylsulfoxide mixture
220
-
N-acetyl-L-Tyr-ethyl ester
-
20C, pH 8.0, in non-denaturating water-ethanol mixture
0.1
-
N-acetyl-L-Tyr-p-nitroanilide
-
20C, pH 8.0, in non-denaturating water-dimethylsulfoxide mixture
0.19
-
N-acetyl-L-Tyr-p-nitroanilide
-
20C, pH 8.0, in non-denaturating water-ethanol mixture
82.8
-
N-Acetyl-L-tyrosine ethyl ester
-
25C, pH 7.5
119.5
-
N-Acetyl-L-tyrosine ethyl ester
-
25C, pH 7.5
120
-
N-Acetyl-L-tyrosine ethyl ester
-
25C, pH 7.5
0.611
-
N-alpha-benzoyl-DL-arginine-p-nitroanilide
-
-
43
-
N-benzoyl-L-Tyr ethyl ester
-
at 10C
-
100
-
N-benzoyl-L-Tyr ethyl ester
-
at 35C
-
117
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 10C
-
120
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form B, at 10C
-
142
-
N-benzoyl-L-Tyr ethyl ester
-
at 35C
-
207
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 25C
-
214
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form B, at 32C
-
276
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form B, at 35C
-
329
-
N-benzoyl-L-Tyr ethyl ester
-
enzyme form A, at 35C
-
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
-
25C, 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
45.9
-
N-benzoyl-L-tyrosine ethyl ester
-
25C, pH 7.5
70.4
-
N-benzoyl-L-tyrosine ethyl ester
-
25C, 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 10C
0.1
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A and enzyme form B, at pH 10C
0.3
-
N-benzoyl-Tyr p-nitroanilide
-
at 25C
0.41
-
N-benzoyl-Tyr p-nitroanilide
-
at 35C
0.41
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A, 25C
0.42
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form B, at 25C
0.72
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form B, at 25C
0.82
-
N-benzoyl-Tyr p-nitroanilide
-
enzyme form A, at 35C
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
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8
0.017
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8, in the presence of 10 mM tetrabutylammonium bromide
0.025
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8, in the presence of 1000 mM tetrabutylammonium bromide
0.034
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8, in the presence of 2 mM NaClO4
0.039
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8, in the presence of 2.5 mM NaCl
0.31
-
N-glutaryl-L-Phe-p-nitroanilide
-
25C, pH 7.8, in the presence of 400 mM tetrabutylammonium bromide
0.014
-
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.05
-
N-succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.031
0.51
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
8.04
-
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
16
-
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.006
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.01
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M LiCl
0.026
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M KCl
0.26
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.27
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 800 mM NaF
0.34
-
N-succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaBr
1.45
-
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
15
-
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
12
-
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
18
-
N-succinyl-Ala-Ala-Pro-Nle-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
0.04
1.97
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
3.3
-
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
5.32
-
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
9.31
-
N-succinyl-Ala-Ala-Pro-Nva-p-nitroanilide
-
21C, 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
10.58
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
chymotrypsin 4
77
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2, 3 M NaCl
110
-
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
21C, pH 8.3, 20 mM CaCl2
0.9
-
N-succinyl-Ala-Phe-Ala
-
30C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide
1.2
-
N-succinyl-Ala-Phe-Ala
-
30C, pH 8.0, HPLC-based assay
0.65
-
N-succinyl-Ala-Phe-p-nitroanilide
-
30C, pH 8.0
39
-
N-succinyl-L-Ala-Ala-Phe-p-nitroanilide
-
at 25C
18.6
-
N-succinyl-L-Ala-Ala-Pro-p-nitroanilide
-
in 50 mM Tris-HCl pH 8.0 with 10 mM CaCl2, at 30 C
7.8
-
N-succinyl-L-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 25C
0.014
-
N-succinyl-L-Phe-p-nitroanilide
-
at 25C
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
0.6
-
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
-
p-nitrophenyl acetate
-
in 20 mM Tris/HCl pH 7.5 at 25C
0.028
-
p-nitrophenyl acetate
-
in the presence of 20 mM hexadecyltrimethylammonium bromide, in 20 mM Tris/HCl pH 7.5 at 25C
98.3
-
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
37C, pH 8.0
4.8
-
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 30C, chymotrypsin II
18.6
-
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
at 30C, chymotrypsin I
105
-
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
-
37C, pH 8.0
1.9
-
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30C
0.9
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37C
2.7
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin A, at pH 7.5 and 37C
3.4
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin B, at pH 7.5 and 37C
3.04
-
benzoyl-D-Leu-4-guanidinophenyl ester
-
25C, pH 7.6
additional information
-
benzoyl-D-Phe-4-guanidinophenyl ester
-
25C, pH 7.6
76.6
-
benzoyl-Tyr ethyl ester
-
-
additional information
-
additional information
-
influence of dimethylsulfoxide on the turnover-number
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
21
-
succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide
-
at 30C
302506
1100
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
at pH 7.5 and 37C
34549
1900
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin A, at pH 7.5 and 37C
34549
6800
-
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
chymotrypsin B, at pH 7.5 and 37C
34549
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.08
-
(Cbz-alanyl)aminomethyl boronic acid
-
37C, pH 8.0
1.96
-
(Cbz-phenylalanyl)aminomethyl boronic acid
-
37C, pH 8.0
1e-05
-
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
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
31.01
-
4-fluorophenylboronic acid
-
37C, pH 8.0
0.3363
-
5'-demethoxyepiexcelsin
-
-
-
0.00057
-
Ac-Phe-Val-Thr-p-amino-L-phenylalanine-CHO
-
-
3.2e-06
-
Ac-Phe-Val-Thr-p-nitro-L-phenylalanine-CHO
-
-
1.1e-05
-
Ac-Phe-Val-Thr-Phe-CHO
-
-
0.001
-
Ac-Phe-Val-Thr-pyridyl-L-alanine-CHO
-
-
1.7e-06
-
Ac-Phe-Val-Thr-Tyr-CHO
-
-
1e-05
-
Acacia plumosa trypsin inhibitor A
-
in phosphate buffer saline, pH 7.4, at 37C for 30 min
-
1.02e-05
-
Acacia plumosa trypsin inhibitor B
-
in phosphate buffer saline, pH 7.4, at 37C for 30 min
-
1.09e-05
-
Acacia plumosa trypsin inhibitor C
-
in phosphate buffer saline, pH 7.4, at 37C for 30 min
-
3.5e-10
-
anti-trypsin-chymotrypsin A
-
-
-
4e-10
-
anti-trypsin-chymotrypsin B
-
-
-
7.5e-06
-
Aprotinin
-
25C, pH 7.5
1.8e-05
-
Aprotinin
-
25C, pH 7.5
9.9e-07
-
AVPGSWPW
-
-
0.344
-
benzyloxycarbonyl-Ala-Ala-Phe-glyoxal
-
at 25C
2.5e-05
-
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 25C
0.024
-
benzyloxycarbonyl-Ala-Pro-Phe-glyoxal
-
at pH 7.17 and 25C
0.065
-
benzyloxycarbonyl-Phe-glyoxal
-
-
0.00085
-
benzyloxycarbonyl-Pro-Phe-glyoxal
-
37, pH 7.4
2e-05
-
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
4.5e-05
-
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
-
-
0.014
-
complex of vanadate and benzohydroxamic acid
-
in 20 mM sodium cacodylate (pH 7.4) and 75% saturated ammonium sulfate
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
0.02229
-
epiexcelsin
-
-
-
0.03
-
faradiol 3-O-myristate
-
-
0.058
-
faradiol 3-O-palmitate
-
-
0.0047
-
GAW
-
-
2.7e-08
-
IVNGEEAVPGSWPW
-
-
0.00013
-
Lima bean trypsin inhibitor
-
25C, pH 7.5
-
0.00017
-
Lima bean trypsin inhibitor
-
25C, pH 7.5
-
0.057
-
lup-20(29)-ene-3beta,16beta-diol
-
-
0.026
-
maniladiol 3-O-myristate
-
-
0.12
-
maniladiol 3-O-palmitate
-
-
0.0052
-
micropeptin 478-A
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.072
-
micropeptin 478-B
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.1
-
micropeptin HU1021
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.1
-
micropeptin HU1041
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.1
-
micropeptin HU1069
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.0196
-
micropeptin HU895A
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.0054
-
micropeptin HU895B
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.0028
-
micropeptin HU909
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.024
-
micropeptin HU975
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
0.0182
-
micropeptin HU989
-
at 37C, in 50 mM Tris-HCl buffer, 100 mM NaCl, 1 mM CaCl2 and 1 mM HCl
1e-05
-
mixed monolayer protected gold cluster
-
-
-
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
5e-05
-
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
1.12e-05
-
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
-
37C, pH 8.0
0.00067
-
Soybean trypsin inhibitor
-
25C, pH 7.5
-
0.0019
-
Soybean trypsin inhibitor
-
25C, pH 7.5
-
7.4e-05
-
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
0.003
-
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
0.072
-
tirucalla-7,24-dien-3beta-ol
-
-
3.4e-05
-
TPGVY
-
-
0.11
-
urs-12-ene-3beta,16beta-diol
-
-
1.88e-06
-
winged bean chymotrypsin-trypsin inhibitor
-
Dixon plot analysis, same for recombinant inhibitor and inhibitor obtained from winged bean seeds
-
7.2e-06
-
WSCI
-
-
9.4e-06
-
WSCI
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium (V)
-
above 0.025 mM
0.025
-
(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
-
above 0.025 mM
0.008
-
Acacia confusa chymotrypsin inhibitor
-
-
-
0.025
-
aceto[2,6-bis[(butylthio-jS)methyl]phenyl-kappaC]-,(SP-4-3)-palladium(II)
-
above 0.025 mM
0.025
-
chloro[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
-
above 0.025 mM
7e-05
-
MG-132
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00084
-
N-(tert-butoxycarbonyl)-L-alanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00428
-
N-(tert-butoxycarbonyl)-L-alanyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.0015
-
N-(tert-butoxycarbonyl)-L-leucyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00147
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00054
-
N-(tert-butoxycarbonyl)glycyl-N1-benzyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00028
-
N-(tert-butoxycarbonyl)glycyl-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00274
-
N-(tert-butoxycarbonyl)glycyl-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00038
-
N-benzoyl-L-tyrosine ethyl ester
-
-
0.00451
-
N2-(tert-butoxycarbonyl)-N4-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-aspartamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.01
-
N2-(tert-butoxycarbonyl)-N5-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N1-(naphthalen-2-ylmethyl)-L-glutamamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.00412
-
N2-(tert-butoxycarbonyl)-N6-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N-(naphthalen-2-ylmethyl)-6-oxo-L-lysinamide
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
2e-05
-
PS-341
-
at 37C for 1 h, in 20 mM Tris buffer, pH 8.0, 0.5 mM EDTA and 0.035% SDS
0.0148
-
trypsin-inhibitor
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0034
-
-
casein proteolysis
0.3221
-
-
N-succinyl-L-alanyl-L-alanyl-L-prolinyl-L-phenylalanine p-nitroanilide
0.62
-
-
crude extract
4.1
-
-
after ammonium sulfate fractionation, 6.6fold purified enzyme
6
-
-
crude extract, at 30C
36
-
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, on the amide substrate
39
-
-
chymotrypsin II, on the amide substrate, at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2
43
-
-
after 7.1fold purification, at 30C
44.6
-
-
hydrolysis of N-alpha-acetyl-L-tyrosine ethyl ester
58
-
-
chymotrypsin I, on the amide substrate, at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2
78.4
-
-
hydrolysisi of N-benzoyl-L-tyrosine ethyl ester
84
-
-
at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2, on the ester substrate
109
-
-
chymotrypsin II, on the ester substrate, at 25C, in 50 mM Tris-HCl buffer and 10 mM CaCl2
128
-
-
activated extract
154
-
-
enzyme form A
168
-
-
chymotrypsin I, on the ester substrate, at 25C, pH 8.0, in 50 mM Tris-HCl buffer and 10 mM CaCl2
178
-
-
enzyme form B
500
-
-
affinity chromatography on CMTI in the presence of 5 M NaCl, peak B
581.6
-
-
chymotrypsin B, after gel filtration, 938.1fold purified enzyme
981.8
-
-
chymotrypsin A, after gel filtration, 1583fold purified enzyme
1573
-
-
affinity chromatography on CMTI (isolation of Chtr1)
1800
-
-
affinity chromatography on CMTI in the presence of 5 M NaCl, peak A
additional information
-
-
-
additional information
-
-
-
additional information
-
-
Kh1: 0.25 units with milk-acetate mixture substrate before purification and 1.3 units with milk-acetate mixture substrate after 5.2fold purification at 35C, Kh2: 0.25 units with milk-acetate mixture substrate before purification and 1.8 units with milk-acetate mixture substrate after 7.2fold purification at 35C, Kh3: 0.25 units with milk-acetate mixture substrate before purification and 4.1 units with milk-acetate mixture substrate after 16.4fold purification at 35C (1 unit is defined as the amount of enzyme that clots 5 ml of milk-acetate mixture during 1 min)
additional information
-
-
the activity towards the most reactive (S)-enantiomer in octane increased 440-fold, increasing the molar ratio of PEG-to-enzyme from 1.1 to 7.1 results in a more than 2fold decrease in enzyme activity
additional information
-
-
no hydrolysis of N-benzoyl-L-tyrosine p-nitroanilide
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
when immobilized on on magnetic nanogels
7.5
-
Q1M0X9
-
7.8
-
-
hydrolysis of N-benzoyl-L-Tyr ethyl ester
7.8
-
-
hydrolysis of N-benzoyl-L-Tyr ethyl ester
7.8
-
-
-
7.8
-
-
hydrolysis of benzoyl-Tyr ethyl ester
7.9
-
-
using N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-metyhlcoumarin as a substrate
8
-
-
hydrolysis of casein
8
-
-
hydrolysis of N-benzoyl-L-tyrosine ethyl ester
8
-
-
-
8
-
-
degradation of deltamethrin by chymotrypsin
8
-
-
at 25C, with succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide as substrate
8
-
-
chymotrypsin I and II, at 25C, with succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrate
8.6
10
-
-
9
-
-
-
9.5
-
-
chymotrypsin isoform Kh2; chymotrypsin isoform Kh3
9.5
-
-
using N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-metyhlcoumarin as a substrate
10.5
11
-
-
10.5
-
-
chymotrypsin isoform Kh1
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
11
-
low activity of chymotrypsin I and II at acidic pH (4-5), considerably activity at pH from 6 to 9 whilst chymotrypsin I shows the highest activity toward the alkaline pH (7-11)
4
9
-
chymotrypsin isoform Kh2
4
9
-
low activity chymotrypsin I and II at acidic pH (45), considerably activity at pH from 6 to 9
4.5
9.8
-
approx. 1% of maximal activity at pH 4.5, approx. 5% of maximal activity at pH 9.8
5
10
-
retains more than 80% activity over the pH range 5-10
5
7
-
chymotrypsin isoform Kh3
5
9
-
chymotrypsin isoform Kh1
6
9.3
-
pH 6.0: about 35% of maximal activity, pH 9.3: 40% of maximal activity
6.5
9.5
-
about 30% of maximal activity at pH 6.5 and at pH 9.5
additional information
-
-
optimal pH of chymotrypsin A and B are 7.5 and 8.0, respectively, at 37C
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35.8
-
-
-
37
-
-
temperature-dependent efficiency of catalysis reveals a bell-shaped feature with a peak at 37C
45
50
-
activity of chymotrypsin I and II increases with temperature up to an optimum of 50 and 45C, respectively, when assayed against succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at pH 8.0
50
-
-
-
55
-
-
-
55
-
-
activity increases with temperature up to an optimum of 55C, when assayed against succinyl-L-Ala-Ala-Pro-L-phenylalanine-p-nitroanilide at pH 8
58
-
-
after modification of alpha-chymotrypsin with mono-6-formyl-beta-cyclodextrin and mono-6-succinyl-6-deoxy-beta-cyclodextrin
additional information
-
-
optimum temperatures of chymotrypsin A and B are 40 and 50C, respectively, at pH 7.5 using 0.1 M Tris-HCl buffer
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
45
-
-
10
50
-
chymotrypsin I shows high activity in the range from 20C to 50C and chymotrypsin II from 10C to 45C
20
45
-
chymotrypsin A at 20C exhibits more than 60% of its maximum activity, which is much higher than chymotrypsin B (27%). Slight changes in activity for both enzymes at 37C. Relative activities of the two enzymes decrease sharply at above 45C
20
62
-
approx. 50% of maximal activity at 20C, approx. 20% of maximal activity at 62C
37
40
-
catalytic activity of the enzyme exponentially falls off after 40C and is thought to be associated with the thermal denaturation of the protein, the kcat and KM values associated with the enzyme catalysis increase up to 40C and then fall
55
70
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
-
-
pI about 4.3, isoelectric focusing
4.3
-
-
chymotrypsin I, electrofocusing
4.93
-
-
chymotrypsin isoform Kh1
5.23
-
-
chymotrypsin isoform Kh2
5.8
-
-
chymotrypsin II, electrofocusing
6.18
-
-
chymotrypsin isoform Kh3
8.8
-
-
-
10.5
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
first-instar larvae
Manually annotated by BRENDA team
-
lung cancer cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
light scattering analysis
23600
-
-
gel filtration
23800
-
-
gel filtration
25000
-
-
-
25000
-
-
SDS-PAGE
25210
-
-
MALDI-TOF analysis
25500
-
-
gel filtration
26000
-
-
gel filtration
26000
-
-
SDS-PAGE
27000
-
-
SDS-PAGE
28000
-
P07338
SDS-PAGE
39800
-
-
Sephadex G-75 superfine gel chromatography
48000
-
Q7SIG2
chymotrypsin C1 migrates on SDS-PAGE as a very stable dimer of 48000 Da
additional information
-
Q1M0X9
SDS-PAGE of partial purified chymotrypsin results in the resolution of bands of 31 and 29 kDa, in addition to others with masses lower than 14 kDa
additional information
-
-
43000, recombinant winged bean chymotrypsin-trypsin inhibitor in complex with chymotrypsin, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 26309, calculation from amino acid analysis
?
-
x * 24000, enzyme form LCTa, SDS-PAGE; x * 25000, enzyme form LCTb, SDS-PAGE; x * 26990, enzyme form LCTb, SDS-PAGE
?
-
x * 24000, SDS-PAGE; x * 24852, calculation from nucleotide sequence
?
-, Q9Y843
x * 18499, deduced from nucleotide sequence
?
-
x * 28000, chymotrypsin A, SDS-PAGE. X * 27000, chymotrypsin B, SDS-PAGE
?
-
x * 24000, SDS-PAGE
dimer
Q7SIG2
2 * 24061, MALDI mass spectroscopy
monomer
-
1 * 26000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
alpha-chymotrypsinogen is formed from chymotrypsinogen A by cleavage of the peptide bond Ser13-Arg15 and Thr147-Asn148
proteolytic modification
-
zymogen: chymotrypsinogen
proteolytic modification
-
optimal autoactivation at pH 7.5
glycoprotein
-
covalent modification with methoxy-polyethylene glycol
proteolytic modification
-
enzyme is secreted in the pancreas as chymotrypsinogen, the single-chain protein of 245 amino acids is activated to chymotrypsinogen by hydrolysis of a single peptide bond, catalyzed by trypsin
proteolytic modification
-
autolytic inactivation at autolytic sites Phe114, Tyr146 and Asn147
proteolytic modification
-
zymogen: chymotrypsinogen
additional information
-
chemical modification of the surface exposed lysine amino groups of alpha-CT with activated poly(ethylene glycol)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-chymotrypsin/eglin c complex at 2.6 A resolution
-
alpha-chymotrypsin:Kunitz-inhibitor complex
-
chymotrypsin complexed to the inhibitors domain of Alzheimer's amyloid beta-protein precursor, APPI, and basic pancreatic trypsin inhibitor, engineering of inhibitors with altered specificities
-
crystals are grown from 52% ammonium sulfate as precipitant containing 10 mg/ml of gamma-chymotrypsin, 100 mM sodium-cacodylate, pH 7.0 and 2.5% dioxane using the hanging-drop vapor diffusion method, crystals of gamma-chymotrypsin complexed with 7-hydroxycoumarin diffract to 1.8 A
-
crystals of chymotrypsin complexed with the inhibitor Leu-Phe-p-fluorophenylmethylamide
-
hanging drop vapour diffusion method
-
hanging drop vapour diffusion method in 10 mM sodium cacodylate pH 6.0, 0.75% saturated cetyltrimethylammonium bromide, 45% saturated ammonium sulfate, and 1 M NaI solution
-
hanging-drop method
-
in complex with the black-eyed pea trypsin/chymotrypsin inhibitor, by hanging drop vapour diffusion method with 0.1 M HEPES pH 7.5, 10% (w/v) polyethylene glycol 6000, and 5% (v/v) 2-methyl-2,4-pentanediol as precipitant
P00766
hanging drop vapour diffusion method with 25% PEG 8000, 0.2 M ammonium sulfate, 15% glycerol
-
hanging drop vapour diffusion method with 0.1 M HEPES pH 7.0 as precipitant solution containing 30% PEG6000
-
hanging drop vapor diffusion, diffraction-quality crystals are grown from droplets containing an equal mixture of inhibited protein and precipitant, i.e. 100 mM PIPES, 1.6 M ammonium sulfate, pH 6.5, crystals diffract to 1.7 A
Q7SIG2
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
5C, about 55% loss of activity after 60 min
3
-
-
5C, about 65% loss of activity after 60 min
4
-
-
5C, about 30% loss of activity after 60 min
5
12
-
5C, stable for 60 min
5
8
-
high stability at pH 7-8, unstable below pH 5
6
11
-
chymotrypsin I and chymotrypsin II, are most stable at alkaline pH
6
11
-
chymotrypsin A and B. The two chymotrypsins are unstable at pH below 5.0, about 10% activity for the enzymes at pH 4.0
7.4
-
-
25C, stable for at least 10 h
additional information
-
-
effect of pH variation on protein adsorption through atomic forcemicroscopy (AFM) measurements in liquid
additional information
-
-
is stable at acid and alkaline pH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
-
activity quickly decreases at temperatures above the optimum, the relative activity of the enzyme at 25C is 60% of maximum activity, the enzyme is labile at high temperatures (more than 55C) and stabilized at less than 30C
25
60
-
rapid inactivation above 60C
25
-
-
retaining around 85% of the initial activity after 2 h
35
55
-
approx. 50% loss of activity after 10 min at 50C, complete loss of activity after 10 min at 55C
40
-
-
is inactivated at 60C
40
-
-
chymotrypsin I is completely inactivated at 55C and chymotrypsin II at 50C
49.5
-
-
melting temperature
52.8
-
-
melting temperature
75
85
-
almost no activity is retained when the incubation temperature is above 75C, the activity of the nanogel-bound alpha-CT still has a residual activity of 88.7% at 85C
additional information
-
-
thermostability of alpha-chymotrypsin is enhanced by about 4-6C after modification with mono-6-formyl-beta-cyclodextrin and mono-6-succinyl-6-deoxy-beta-cyclodextrin
additional information
-
-
significant improvement in thermal stability of chymotrypsin is achieved after the covalent attachment of the enzyme on chitosan. The half-life of immobilized chymotrypsin can be increased from 0.57 h, at 55C, to 7.8 h, at 65C
additional information
-
-
thermodynamic unfolding experiments reveal that PEGylation increases the thermal transition temperature (Tm) of alpha-CT by up to 6C and the free energy of unfolding [DELTAGU (25C)] by up to 5 kcal/mol
additional information
-
-
native bovine chymotrypsin rapidly loses activity when incubated at 55C. Glycosylated chymotrypsin has greatly increased thermostability compared to the native enzyme, after incubation at 50C and pH 8.0, glycosylated bovine chymotrypsin retains 45% of its original activity and the native enzyme is inactivated
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-chymotrypsin immobilized on mesoporous silica is stable for at least 1 week, i.e. 20 recycles per day, at room temperature, activity decreases gradually to 15% during next 10 days
-
enzyme stability is analyzed in 0.05 M Tris-HCl buffer pH 8.20 in the presence or the absence of methylamine, urea or methylamine + urea mixture of various concentrations at 25C for 4 h to attain complete equilibrium. Indication that methylamines suppress the aggregation of a thermal denatured protein and that methylamines have comparable effects on counteracting the temperature-perturbing actions on alpha-chymotrypsin.
-
in the presence of putrescine and spermidine a clear stabilizing effect against thermal unfolding is achieved
-
lanthanide ions, e.g. terbium accelerates the inactivation process
-
protects the enzyme from inactivation process, probably of autolytic nature
-
Ca2+ stabilizes the enzyme near pH 7, at low pH the enzyme is more stable in absence of Ca2+
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetonitrile
-
approx. 50% loss of activity after 20 min at 25C in 70% acetonitrile, complete loss of activity after 20 min at 25C in 75% acetonitrile, approx. 40% loss of activity after 20 min at 25C in 95% acetonitrile
dioxane
-
approx. 50% loss of activity after 20 min at 25C in 20% 1,4-dioxane, complete loss of activity after 20 min at 25C in 60% 1,4-dioxane, approx. 80% loss of activity after 20 min at 25C in 95% 1,4-dioxane
Ethanol
-
approx. 50% loss of activity after 20 min at 25C in 20% ethanol, complete loss of activity after 20 min at 25C in 40% ethanol, approx. 60% loss of activity after 20 min at 25C in 95% ethanol
Ethanol
-
approx. 50% loss of activity after 5 min at 25C in 60% ethanol, almost complete loss of activity after 10 min, approx. 50% loss of activity after 10 min at 25C in 50% ethanol, approx. 50% loss of activity after 15 min at 25C in 40% ethanol, approx. 30% loss of activity after 40 min at 25C in 30% ethanol, no loss of activity after 120 min at 25C in 60% ethanol in the presence of 100 mg/ml polyethylene glycol 2000, approx. 50% loss of activity after 120 min at 25C in 60% ethanol in the presence of 1.4 M D-fructose, 1.24 M D-sorbitol, 700 mM saccharose, or 12.5% glycerol
Ethanol
-
almost complete loss of activity after 10 min in 60% ethanol, no decrease in activity in the presence of 1.2 M CaCl2
Ethanol
-
approx. 60% loss of activity after 20 min in 40% ethanol, complete loss of activity after 20 min in 60% ethanol, 70% loss of activity after 60 min in 60% ethanol in the presence of polyethylene glycol 6000, 12000 or 20000
Ethanol
-
at 50% ethanol alpha-chymotrypsin has an ordinary beta-sheet structure, at 70% or 90% ethanol the structure changes to a native-like, i.e. alpha and beta type, structure
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
25C, free enzyme in 80 mM Tris-HCl at pH 7.8, 22 days, complete loss of activity
-
25C, nanogel-immobilized enzyme, 36 days, about 10% loss of activity
-
25C, tetrabutylammonium bromide, 2 months, 30% loss of activity
-
4C, free enzyme in 80 mM Tris-HCl at pH 7.8, 36 days, 16.5% loss of activity
-
0C, stable for months
-
4C, enzyme form LCTa is very susceptible to autolysis, enzyme form LCTb is more stable but undergoes considerable breakdown if stored for more than 3-4 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration
-
use of Sepharose-immobilized denatured alpha-chymotrypsin for purification
-
anion exchange column, cation exchange column, affinity F2
-
chymotrypsin A and B, to homogeneity by ammonium sulfate fractionation and gel filtration
-
recombinant CHY1
-, Q9Y843
SB-TI-Sepharose column chromatography
P07338
SBTI-Sepharose column chromatography and HiPrep Sephacryl-100 column gel filtration
-
chymotrypsin I and II, by ionic exchange chromatography
-
ammonium sulfate fractionation, Sephadex G-75 gel filtration, and DEAE-Sepharose column chromatography
-
gel filtration and ion exchange chromatography
-
affinity chromatography
-
use of Sepharose-immobilized denatured alpha-chymotrypsin for purification
-
4 insect chymotrypsins from 3 different insect orders (Dictyoptera, Coleoptera, and two Lepidoptera) are isolated using affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Pichia pastoris
-
expressed in Escherichia coli
-
enzyme form LCTb
-
expression of cDNA in Pichia pastoris
-, Q9Y843
expressed in Escherichia coli BL21 (DE3) pLysS cells
P07338
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F114I
-
autolytic site
Y146H
-
autolytic site
Y146H/N147S
-
autolytic sites, altered routes of autolytic degradation
additional information
-
selective oxidation of Met192 to its sulfoxide derivative leads to changes of catalytic parameters for the hydrolysis of synthetic substrates and thermodynamic and kinetic interactions with the macromolecular inhibitor eglin c
additional information
-
alpha-chymotrypsin is chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700 (PEG700-alpha-chymotrypsin), 2000 (PEG2000-alpha-chymotrypsin), and 5000 Da (PEG5000-alpha-chymotrypsin)) and the amount of polymer attached to the enzyme is varied systematically from 1 to 9 PEG molecules per enzyme molecule
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
chymotrypsin and potentially other serine proteases could be attractive candidates for the development of biocatalyst for the control of residual pesticides in the environment and on agricultural products
drug development
-
enediyne-amino acid conjugates as potent inhibitors of alpha-chymotrypsin
drug development
-
winged bean chymotrypsin-trypsin inhibitor is a dual inhibitor of both chymotrypsin and trypsin and a promising candidate to study for its insecticidal properties against Helicoverpa armigera and other insect pests
drug development
-
design of a new class of boron peptides as inhibitors of the chymotrypsin-like activity of the 20S proteasome based around the structure of Belactosin C, proteasome inhibitors with therapeutic utility
medicine
-
pancreatitis treatment
synthesis
-
reaction catalyzer in apolar organic solvents
biotechnology
-
dependence of activity on pH and temperature makes chymotrypsin II a biotechnological alternative for food processing when low temperatures are needed like in fish ripening, fish sauce production, fish protein hydrolysate production and other emerging processes. This enzyme together with other proteases from sardine viscera may aid in the enzymatic treatment of stick-water, in which a reduction in viscosity is required for further processing of effluent
medicine
-
treatment of gastroenterological diseases
drug development
-
G-quadruplex-scaffold-based receptors are effective inhibitors of ChT by protein-surface recognition. This may provide a general strategy to generate synthetic combinatorial libraries of receptors to target different classes of proteins
synthesis
-
enzymes are often used in organic solvents for catalyzing organic synthesis. Two enzyme preparations, EPRP (enzyme precipitated and rinsed with n-propanol) and PCMC (protein coated microcrystals) show much higher activities than lyophilized powders in such systems. Both preparations involve precipitation by an organic solvent
additional information
-
potential application value of the two chymotrypsins A and B where low processing temperature and higher enzymatic activity is needed