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Ac-L-Lys-4-nitroanilide + H2O
N2-acetyl-L-Lys + 4-nitroaniline
acyl-L-lysine-4-nitroanilide + H2O
acyl-L-lysine + 4-nitroaniline
benzoyl-Arg ethyl ester + 3-amino-propionamide
ethanol + benzoyl-Arg-3-amino-propionamide
-
-
-
?
benzoyl-Arg ethyl ester + 3-amino-propionic acid methyl ester
ethanol + benzoyl-Arg-3-amino-propionic acid methyl ester
-
-
-
?
benzoyl-Arg ethyl ester + 4-amino-butyramide
ethanol + benzoyl-Arg-4-amino-butyramide
-
-
-
?
benzoyl-Arg ethyl ester + 4-amino-butyric acid methyl ester
ethanol + benzoyl-Arg-4-amino-butyric acid methyl ester
-
-
-
?
benzoyl-Arg ethyl ester + 5-amino-pentanoic acid
ethanol + benzoyl-Arg-5-amino-pentanoic acid
-
-
-
?
benzoyl-Arg ethyl ester + 5-amino-pentanoic acid amide
ethanol + benzoyl-Arg-5-amino-pentanoic acid amide
-
-
-
?
benzoyl-Arg ethyl ester + 5-amino-pentanoic acid methyl ester
ethanol + benzoyl-Arg-5-amino-pentanoic acid methyl ester
-
-
-
?
benzoyl-Arg ethyl ester + 6-amino-hexanoic acid
ethanol + benzoyl-Arg-6-amino-hexanoic acid
-
-
-
?
benzoyl-Arg ethyl ester + 6-amino-hexanoic acid amide
ethanol + benzoyl-Arg-6-amino-hexanoic acid amide
-
-
-
?
benzoyl-Arg ethyl ester + 6-amino-hexanoic acid methyl ester
ethanol + benzoyl-Arg-6-amino-hexanoic acid methyl ester
-
-
-
?
benzoyl-Arg ethyl ester + 9-amino-nonanoic acid
ethanol + benzoyl-Arg-9-amino-nonanoic acid
-
-
-
?
benzoyl-Arg ethyl ester + 9-amino-nonanoic acid amide
ethanol + benzoyl-Arg-9-amino-nonanoic acid amide
-
-
-
?
benzoyl-Arg ethyl ester + 9-amino-nonanoic acid methyl ester
ethanol + benzoyl-Arg-9-amino-nonanoic acid methyl ester
-
-
-
?
benzoyl-L-Arg-4-nitroanilide + H2O
benzoyl-L-Arg + 4-nitroaniline
benzoyl-Lys-4-nitroanilide + H2O
benzoyl-Lys + 4-nitroaniline
benzoyl-Phe 4-guanidinephenyl ester + 2-amino-4-methyl-pentan-1-ol
4-guanidinephenol + benzoyl-Phe-2-amino-4-methyl-pentan-1-ol
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + 3-amino-propane-1,2-diol
4-guanidinephenol + benzoyl-Phe-3-amino-propane-1,2-diol
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + 3-amino-propanol
4-guanidinephenol + benzoyl-Phe-3-amino-propanol
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + 5-amino-pentanol
4-guanidinephenol + benzoyl-Phe-5-amino-pentanol
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + cycloheptylamine
4-guanidinephenol + benzoyl-Phe-cycloheptylamide
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + pentylamine
4-guanidinephenol + benzoyl-Phe-pentylamide
-
-
-
?
benzoyl-Phe 4-guanidinephenyl ester + propylamine
4-guanidinephenol + benzoyl-Phe-propylamide
-
-
-
?
carbobenzoxy-Arg methyl ester + L-Pro-NH2
carbobenzoxy-Arg-Pro-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
?
carbobenzoxy-L-Arg methyl ester + D-Phe-NH2
carbobenzoxy-Arg-D-Phe-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
-
?
carbobenzoxy-L-Arg methyl ester + D-Trp-NH2
carbobenzoxy-Arg-D-Trp-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
-
?
carbobenzoxy-L-Arg methyl ester + Gly-NH2
carbobenzoxy-Arg-Gly-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
-
?
carbobenzoxy-L-Arg methyl ester + L-Phe-NH2
carbobenzoxy-Arg-Phe-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
-
?
carbobenzoxy-L-Arg methyl ester + L-Trp-NH2
carbobenzoxy-Arg-Trp-NH2 + methanol
-
no activity with carbobenzoxy-D-Arg methyl ester
-
-
?
cholecystokinin + H2O
cholecystokinin 8
-
cleavage of large forms of cholecystokinin
-
?
histone H3 + H2O
?
-
-
-
-
?
histone H4 + H2O
?
-
-
-
-
?
L-Arg methyl ester + H2O
L-Arg + methanol
-
-
-
-
?
maleyl-Tyr-Arg ethyl ester + H2O
?
-
-
-
-
?
N-benzoyl-Arg amide + H2O
N-benzoyl-Arg + NH3
-
-
-
-
?
N-benzoyl-Arg benzyl ester + H2O
N-benzoyl-Arg + benzyl alcohol
-
-
-
-
?
N-benzoyl-Arg ethyl ester + H2O
N-benzoyl-Arg + ethanol
-
-
-
-
?
N-benzoyl-Arg isopropyl ester + H2O
N-benzoyl-Arg isopropanol
-
-
-
-
?
N-benzoyl-Arg methyl ester + H2O
N-benzoyl-Arg + methanol
-
-
-
-
?
N-benzoyl-DL-arginine 4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-Benzoyl-L-Arg ethyl ester + H2O
N-Benzoyl-L-Arg + ethanol
-
-
-
?
Nalpha-benzoyl-Arg p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
Nalpha-benzoyl-L-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
Nalpha-benzoyl-L-Lys methyl ester + H2O
Nalpha-benzoyl-L-Lys + methanol
-
-
-
-
?
Nalpha-benzoyl-Lys methyl ester + H2O
Nalpha-benzoyl-Lys + methanol
-
-
-
-
?
Nalpha-p-tosyl-Arg amide + H2O
Nalpha-p-tosyl-Arg + NH3
-
-
-
-
?
p-nitrophenyl p-guanidinobenzoate + H2O
p-nitrophenol + p-guanidinobenzoate
-
-
-
-
?
p-tosyl-Arg methyl ester + H2O
p-tosyl-Arg + methanol
parvalbumin + H2O
?
-
exclusive cleavage of the Arg75-Ala76 bond
-
-
?
proinsulin fusion protein + H2O
insulin + ?
-
clostripain specifically cleaves the arginine residues in the leader peptide and in the C-peptide
-
-
?
succinyl-CoA synthetase + H2O
?
-
the mutant forms of E. coli succinyl-CoA synthetase, W76F and W43,76,248F are more sensitive to proteolysis by clostripain than the wild-type enzyme. No influence of phosphorylation or dephosphorylation state. Argbeta80 is the principal site of inactivation by clostripain
-
-
?
Thr-Ala-Ala + H2O
?
-
-
-
-
?
additional information
?
-
Ac-L-Lys-4-nitroanilide + H2O
N2-acetyl-L-Lys + 4-nitroaniline
-
-
-
-
?
Ac-L-Lys-4-nitroanilide + H2O
N2-acetyl-L-Lys + 4-nitroaniline
-
-
-
-
?
acyl-L-lysine-4-nitroanilide + H2O
acyl-L-lysine + 4-nitroaniline
-
-
-
?
acyl-L-lysine-4-nitroanilide + H2O
acyl-L-lysine + 4-nitroaniline
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzoyl-L-Arg-4-nitroanilide + H2O
benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-L-Arg-4-nitroanilide + H2O
benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-Lys-4-nitroanilide + H2O
benzoyl-Lys + 4-nitroaniline
-
-
-
-
?
benzoyl-Lys-4-nitroanilide + H2O
benzoyl-Lys + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
the enzyme exhibits strict specificity for arginine at the P1 position, the enzyme displays 2fold higher specific activity with N-benzoyl-L-arginine-4-nitroanilide compared to acyl-L-lysine-4-nitroanilide
-
-
?
Nalpha-benzoyl-L-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
the enzyme exhibits strict specificity for arginine at the P1 position, the enzyme displays 2fold higher specific activity with N-benzoyl-L-arginine-4-nitroanilide compared to acyl-L-lysine-4-nitroanilide
-
-
?
p-tosyl-Arg methyl ester + H2O
p-tosyl-Arg + methanol
-
-
-
-
?
p-tosyl-Arg methyl ester + H2O
p-tosyl-Arg + methanol
-
N-alpha-p-tosyl-L-Arg methyl ester
-
-
?
additional information
?
-
-
cleaves proteins and synthetic substrates preferentially at the carboxyl group of Arg
-
-
?
additional information
?
-
-
specificity is confined primarily to Arg residues
-
-
?
additional information
?
-
-
the major activity is directed towards the carboxyl peptide linkage of Arg
-
-
?
additional information
?
-
-
clostripain enhanced phagocytosis of apoptotic neutrophils by macrophages
-
-
?
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5,5'-dithiobis(2-nitrobenzoate)
-
-
ADP
-
proteolysis of succinyl-CoA synthetase
antipain
-
potent clostridiopeptidase B-induced kinin release in dog plasma
ATP
-
proteolysis of succinyl-CoA synthetase
benzylamidinyl-diazo dichlorotriazine
-
effective protection by N-benzoyl-L-Arg ethyl ester
benzyloxycarbonyl-Phe-Lys-CH2S(CH3)2
-
irreversible
Borate
-
partial inhibition
citrate
-
partial inhibition
diallyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
diallyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
diallyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
diallyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
dibutyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
dibutyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
dibutyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
dibutyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
-
-
diethyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
diethyl-2,4,4-trimethyl-8-nitro-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
-
-
diethyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
diethyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
-
-
diisopropylfluorophosphate
-
-
dimethyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b]-[1,4]diazepin-2-ylphosphonate
-
-
dimethyl-2,4,4-trimethyl-8-nitro-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
-
-
dimethyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
dimethyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
-
-
E-64
-
0.035 mM, 68% inhibition
histatin 5
-
23.6 nM, 50% inhibition, competitive. The salivary protein could be used for the prevention or treatment of topical infactions such as those caused by Clostridium histolyticum
-
iodoacetic acid
-
0.035 mM, 13% inhibition
L-1-chloro-3-[4-tosylamido]-7-amino-2-heptanone
-
complete inhibition
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
i.e. compounds E-64
macroglobulin
-
alpha2-macroglobulin from human plasma, inhibits both the amidase and protease activity. Macroglobulin from rat and dog plasma
-
N-alpha-p-nitrobenzyloxycarbonyl-Arg chloromethyl ketone
-
irreversible
N-Alpha-p-tosyl-L-homoarginine methyl ester
-
-
N-alpha-p-tosyl-L-Lys chloromethyl ketone
N-Alpha-p-tosyl-L-norarginine methyl ester
-
-
N-tosyl-Lys-chloromethylketone
-
0.035 mM, complete inhibition
Nalpha-tosyl-L-lysine chloromethylketone
-
complete inhibition at 0.01 mg/ml
ovoinhibitor
-
0.05 mM, 55% reduced amidase activity
-
phenylmethylsulfonyl fluoride
-
complete inhibition
Polyarginine
-
hydrolysis of benzoyl-Arg ethyl ester
polylysine
-
hydrolysis of benzoyl-Arg ethyl ester
RCM RNase
-
hydrolysis of benzoyl-Arg ethyl ester
-
tosyl-Lys-chloromethane
-
-
Tris
-
partial inhibition
Veronal
-
partial inhibition
additional information
-
no inhibition by 0.035 PMSF
-
benzamidine
-
0.035 mM, 28% inhibition
butylguanidine
-
most effective competitive inhibitor, hydrolysis of benzoyl-Arg ethyl ester
Cd2+
-
-
Cd2+
-
0.01 mM, 30% inhibition
Co2+
-
-
Co2+
-
0.01 mM, 50% inhibition
Cu2+
-
-
Cu2+
-
0.01 mM, 30% inhibition
H2O2
-
complete regeneration by reduction with dithiothreitol
K+
-
-
K+
-
100 mM, 40% inhibition
leupeptin
-
0.035 mM, complete inhibition
leupeptin
-
potent clostridiopeptidase B-induced kinin release in dog plasma
N-alpha-p-tosyl-L-Lys chloromethyl ketone
-
-
N-alpha-p-tosyl-L-Lys chloromethyl ketone
-
competitive
Na+
-
-
Na+
-
100 mM, 40% inhibition
Trypsin inhibitor
-
50% inhibition of amidase activity at 0.04 mM; Kunitz soybean trypsin inhibitor
-
Trypsin inhibitor
-
soy bean trypsin inhibitor, competitive
-
Trypsin inhibitor
-
Kunitz soybean trypsin inhibitor; limabean trypsin inhibitor
-
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0.15
diallyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.032
diallyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.09
diallyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.036
diallyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.175
dibutyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.3
dibutyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
IC50 above 0.3 mM, in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.14
dibutyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.3
dibutyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
IC50 above 0.3 mM, in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.08
diethyl-2,4,4,9-tetramethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.49
diethyl-2,4,4-trimethyl-8-nitro-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.22
diethyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.3
diethyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
IC50 above 0.3 mM, in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.278
dimethyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo-[b]-[1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.3
dimethyl-2,4,4-trimethyl-8-nitro-2,3,4,5-tetrahydro-1H-benzo-[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
IC50 above 0.3 mM, in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.78
dimethyl-7,8-dichloro-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
0.07
dimethyl-7-benzoyl-2,4,4-trimethyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-2-ylphosphonate
Hathewaya histolytica
-
in 100 mM Tris-HCl buffer, pH 7.4, at 37°C
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Nishimura, J.S.; Ybarra, J.; Mann, C.J.; Mitchell, T.
Sensitivity of Escherichia coli succinyl-CoA mutants at Trp beta 76 to clostripain and to trypsin. ADP and ATP protect against cleavage by clostripain at Arg beta 80
J. Biol. Chem.
268
13717-13722
1993
Hathewaya histolytica
brenda
Mitchell, W.M.; Harrington, W.F.
Clostripain
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
699-719
1971
Hathewaya histolytica
-
brenda
Fortier, G.; MacKenzie, S.L.
Substrate- and stereo-specificities in clostripain-catalyzed peptide synthesis
Biotechnol. Lett.
8
873-876
1986
Hathewaya histolytica
-
brenda
Fortier, G.; MacKenzie, S.L.
Peptide bond synthesis by clostridiopeptidase B
Biotechnol. Lett.
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Primary structure of alpha-clostripain light chain
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1984
Hathewaya histolytica
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Gilles, A.M.; Imhoff, J.M.; Keil, B.
alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain
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1979
Hathewaya histolytica
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Giroux, E.; Vargaftig, B.B.
Clostridiopeptidase B inhibition by plasma marcroglobulins and microbial antiproteases
Biochim. Biophys. Acta
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1978
Hathewaya histolytica
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Mitchell, W.M.
Cleavage at arginine residues by clostripain
Methods Enzymol.
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1977
Hathewaya histolytica
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Emd, I.; Keil, B.
Five Sepharose-bound ligands for the chromatographic purification of Clostridium collagenase and clostripain
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Hathewaya histolytica
brenda
Kula, M.R.; Hatef-Haghi, D.; Tauber-Finkelstein, M.; Shaltiel, S.
Consecutive use of omega-aminoalkylagaroses. Resolution and purification of clostripain and collagenase from Clostridium histolyticum
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1976
Hathewaya histolytica
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Siffert, O.; Emd, I.; Keil, B.
Interaction of clostripain with natural trypsin inhibitors and its affinity labeling by Nalpha-p-nitrobenzyloxycarbonyl arginine chlormethyl ketone
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1976
Hathewaya histolytica
brenda
Cole, P.W.; Murakami, K.; Inagami, T.
Specificity and mechanism of clostripain catalysis
Biochemistry
10
4246-4252
1971
Hathewaya histolytica
brenda
Encontre, I.; Parello, J.
Chromatin core particle obtained by selective cleavage of histones H3 and H4 by clostripain
J. Mol. Biol.
202
673-676
1988
Hathewaya histolytica
brenda
Witte, V.; Wolf, N.; Dargatz, H.
Clostripain linker deletion variants yield active enzyme in Escherichia coli: a possible function of the linker peptide as intramolecular inhibitor of clostripain automaturation
Curr. Microbiol.
33
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1996
Hathewaya histolytica
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Mitchell, W.M.; Harrington, W.F.
Purification and properties of clostridiopeptidase B (Clostripain)
J. Biol. Chem.
243
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1968
Hathewaya histolytica
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Kembhavi, A.A.; Buttle, D.J.; Rauber, P.; Barrett, A.J.
Clostripain: characterization of the active site
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283
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1991
Hathewaya histolytica
brenda
Witte, V.; Wolf, N.; Diefenthal, T.; Reipen, G.; Dargatz, H.
Heterologous expression of the clostripain gene from Clostridium histolyticum in Escherichia coli and Bacillus subtilis: maturation of the clostripain precursor is coupled with self-activation
Microbiology
140
1175-1182
1994
Hathewaya histolytica
brenda
Ullmann, D.; Jakubke, H.D.
Kinetic characterization of affinity chromatography purified clostripain
Biol. Chem. Hoppe-Seyler
375
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1994
Hathewaya histolytica
brenda
Beardshall, K.; Deprez, P.; Playford, R.J.; Alexander.M.; Calam, J.
Effect of chymotrypsin on human cholecystokinin release: use of clostripain in the validation of a new radioimmunoassay
Regul. Pept.
40
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1992
Hathewaya histolytica
brenda
Labrou, N.E.; Rigden, D.J.
The structure-function relationship in the clostripain family of peptidases
Eur. J. Biochem.
271
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2004
Hathewaya histolytica
brenda
Gusman, H.; Grogan, J.; Kagan, H.M.; Troxler, R.F.; Oppenheim, F.G.
Salivary histatin 5 is a potent competitive inhibitor of the cysteine proteinase clostripain
FEBS Lett.
489
97-100
2001
Hathewaya histolytica
brenda
Gunther, R.; Stein, A.; Bordusa, F.
Investigations on the enzyme specificity of clostripain: a new efficient biocatalyst for the synthesis of peptide isosteres
J. Org. Chem.
65
1672-1679
2000
Hathewaya histolytica
brenda
Jozwiak, J.; Komar, A.; Jankowska, E.; Martirosian, G.
Determination of the cytotoxic effect of Clostridium histolyticum culture supernatant on HeLa cells in the presence of protease inhibitors
FEMS Immunol. Med. Microbiol.
45
137-142
2005
Hathewaya histolytica
brenda
Guzik, K.; Bzowska, M.; Smagur, J.; Krupa, O.; Sieprawska, M.; Travis, J.; Potempa, J.
A new insight into phagocytosis of apoptotic cells: proteolytic enzymes divert the recognition and clearance of polymorphonuclear leukocytes by macrophages
Cell Death Differ.
14
171-182
2007
Hathewaya histolytica
brenda
Kim, C.K.; Lee, S.Y.; Kwon, O.J.; Lee, S.M.; Nah, S.Y.; Jeong, S.M.
Secretory expression of active clostripain in Escherichia coli
J. Biotechnol.
131
346-352
2007
Clostridium sp.
brenda
Manabe, S.; Nariya, H.; Miyata, S.; Tanaka, H.; Minami, J.; Suzuki, M.; Taniguchi, Y.; Okabe, A.
Purification and characterization of a clostripain-like protease from a recombinant Clostridium perfringens culture
Microbiology
156
561-569
2010
Clostridium perfringens, Clostridium perfringens 13
brenda
Bhattacharya, A.K.; Rana, K.C.; Raut, D.S.; Mhaindarkar, V.P.; Khan, M.I.
An efficient synthesis of benzodiazepinyl phosphonates as clostripain inhibitors via FeCl3 catalyzed four-component reaction
Org. Biomol. Chem.
9
5407-5413
2011
Hathewaya histolytica
brenda
Chakravorty, A.; Awad, M.M.; Hiscox, T.J.; Cheung, J.K.; Carter, G.P.; Choo, J.M.; Lyras, D.; Rood, J.I.
The cysteine protease alpha-clostripain is not essential for the pathogenesis of Clostridium perfringens-mediated myonecrosis
PLoS ONE
6
e22762
2011
Clostridium perfringens, Clostridium perfringens JIR325
brenda
Tanaka, H.; Nariya, H.; Suzuki, M.; Houchi, H.; Tamai, E.; Miyata, S.; Okabe, A.
High-level production and purification of clostripain expressed in a virulence-attenuated strain of Clostridium perfringens
Protein Expr. Purif.
76
83-89
2011
Hathewaya histolytica (P09870), Hathewaya histolytica, Hathewaya histolytica ATCC 19401 (P09870)
brenda
Jankowska-Steifer, E.; Martirosian, G.; Ekiel, A.; Komar, A.; Wiechula, B.; Jozwiak, J.; Cieslik, P.; Moskalewski, S.
Vacuolating, lethal, collagenase and clostripain activities of six reference ATCC Clostridium histolyticum strains
World J. Microbiol. Biotechnol.
27
1689-1694
2011
Hathewaya histolytica, Hathewaya histolytica ATCC 17859, Hathewaya histolytica ATCC 17860, Hathewaya histolytica ATCC 19401, Hathewaya histolytica ATCC 25770, Hathewaya histolytica ATCC 6282, Hathewaya histolytica ATCC 8034
brenda
Brandhorst, H.; Johnson, P.R.; Moench, J.; Kurfuerst, M.; Korsgren, O.; Brandhorst, D.
Comparison of Clostripain and neutral protease as supplementary enzymes for human islet isolation
Cell Transplant.
28
176-184
2019
Hathewaya histolytica (P09870)
brenda
Stahle, M.; Foss, A.; Gustafsson, B.; Lempinen, M.; Lundgren, T.; Rafael, E.; Tufveson, G.; Korsgren, O.; Friberg, A.
Clostripain, the missing link in the enzyme blend for efficient human islet isolation
Transplant. Direct
1
e19
2015
Hathewaya histolytica (P09870)
brenda
Dendo, M.; Maeda, H.; Yamagata, Y.; Murayama, K.; Watanabe, K.; Imura, T.; Inagaki, A.; Igarashi, Y.; Katoh, Y.; Ebina, M.; Fujimori, K.; Igarashi, K.; Ohuchi, N.; Satomi, S.; Goto, M.
Synergistic effect of neutral protease and clostripain on rat pancreatic islet isolation
Transplantation
99
1349-1355
2015
Hathewaya histolytica (P09870), Hathewaya histolytica
brenda