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3-(2-furyl)acryloyl-L-Ala-L-Arg + H2O
3-(2-furyl)acryloyl-L-Ala + L-Arg
-
-
-
?
Arg-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
?
-
bradykinin
-
-
?
benzoyl-beta-Ala-L-Lys + H2O
?
-
low activity
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
benzoyl-Gly-Gly-Phe + H2O
?
-
-
-
-
?
benzoyl-Gly-glycylphenyllactic acid + H2O
?
-
-
-
-
?
benzoyl-Gly-L-Arg + H2O
benzoyl-Gly + L-Arg
-
-
-
-
?
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR + H2O
biotin-(epsilon-aminocaproic acid)2-GLMVGGVV + Arg
-
-
-
?
carbobenzoxy-Gly-L-Phe + H2O
?
-
-
-
-
?
endostar + H2O
?
-
endostar is a derivative of human endostatin that is modified with an additional metal-chelating sequence at the N-terminus. A mixture of carboxypeptidase A and carboxypeptidase B is applied to catalyse the hydrolysis of the C-terminus of apo and holo endostar
-
-
?
Fibrin + H2O
?
-
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA
-
-
?
furylacryloyl-L-alanyl-L-arginine + H2O
furylacryloyl-L-alanine + L-arginine
-
-
-
-
?
furylacryloyl-L-alanyl-L-lysine + H2O
furylacryloyl-L-alanine + L-lysine
-
-
-
-
?
furylacryloylalanylarginine + H2O
?
-
-
-
-
?
furylacryloylalanyllysine + H2O
?
-
-
-
-
?
hippuryl-Gly + H2O
?
-
10% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
hippuryl-L-arginine + H2O
hippuric acid + L-Arg
-
-
-
?
hippuryl-L-Asp + H2O
hippuric acid + L-aspartate
-
hydrolyzed by mutant enzyme D253K and mutant enzyme D253R, wild type enzyme shows no activity
-
-
?
hippuryl-L-Glu + H2O
hippuric acid + Glu
-
hydrolyzed by mutant enzyme D253K, wild type enzyme shows no activity
-
-
?
hippuryl-L-homoarginine + H2O
hippuric acid + homoarginine
-
low activity
-
-
?
hippuryl-L-Lys
hippuric acid + L-Lys
-
-
-
?
hippuryl-L-Orn + H2O
hippuric acid + Orn
-
-
-
-
?
hippuryl-L-Phe + H2O
?
-
18% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-L-Pro-L-Lys + H2O
?
-
low activity
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
hippurylphenyllactic acid + H2O
hippuric acid + phenyllactic acid
-
-
-
-
?
human insulin-like peptide 3 + H2O
?
-
the single-chain precursor of INSL3 is converted to the double-chain mature human INSL3 by endoproteinase Lys-C and carboxypeptidase B treatment. Carboxypeptidase B is added (emzyme/peptide mass ratio 1 : 30) to remove the additional lysine residue at the C-terminus of B-chain
-
-
?
human proinsulin + H2O
?
-
enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process is developed for the reduction of a major derivative, des-threonine human insulin
-
-
?
insulin-like peptide 5 precursor + H2O
?
-
-
-
-
?
Leu-Asp-Ser + H2O
Leu-Asp + Ser
-
-
-
?
mono/di-Arg-insulin + H2O
human insulin
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
N-(4-methoxyphenylazoformyl)-Arg-OH + H2O
?
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe + H2O
?
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
OPN-R + H2O
OPN-L + ?
-
osteopontin (OPN) gets activated by thrombin resulting in OPN-R. OPN-R is subsequently inactivated by CPB generating OPN-L
-
-
?
Val-Asp-Asp-Asp-Lys + H2O
Lys + Asp + ?
-
-
-
?
additional information
?
-
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
mutant enzymes S253K and S253R are inactive
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
129% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
peptidase activity
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
-
?
additional information
?
-
-
hydrolysis of peptide bonds of Lys, Arg, Arn, homoarginine and S-(beta-aminoethyl)cysteine. Esterase activity towards carboxy terminal Arg
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity
-
-
?
additional information
?
-
the enzyme is involved in digestion processes in the gut supplying free amino acid for developing larvae
-
-
?
additional information
?
-
-
the enzyme is involved in digestion processes in the gut supplying free amino acid for developing larvae
-
-
?
additional information
?
-
the enzyme is highly specific for excising C-terminal Lys from peptides and protein substrates
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys from peptides and protein substrates
-
-
?
additional information
?
-
-
the enzyme is specific for COOH-terminal Lys or Arg residues
-
-
?
additional information
?
-
-
the enzyme plays a role in the fibrinolytic or coagulation system
-
-
?
additional information
?
-
-
mechanism for the antifibrinolytic affect of the plasma enzyme
-
-
?
additional information
?
-
-
active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position
-
-
?
additional information
?
-
-
the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity
-
-
?
additional information
?
-
Ser207, Gly253, Tyr248, and Asp255 residues play major role in the substrate recognition by S1-subsite
-
-
?
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(2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
binding structure analysis
(2S)-7-amino-2-[(hydroxy[(1R)-2-methyl-1-[(3-phenylpropanoyl)amino]propyl]phosphoryl)methyl]heptanoic acid
-
(DL-5-guanidinoethyl)mercaptosuccinic acid
-
-
(R)-2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
(R)-2-guanidino-3-mercaptopropanoic acid
-
(S)-2-(2-((S)-1-carboxy-2-(1H-imidazol-5-yl)ethylamino)ethylamino)-5-guanidinopentanoic acid
IC50: 17 microgram/ml
(S)-5-amino-2-((1-propyl-1H-imidazol-4-yl)methyl)pentanoic acid
-
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
2-(2-chloro-5-guanidinophenyl)-3-mercaptopropanoic acid
-
2-(2-guanidinoethylthio)succinic acid
-
2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
2-(4-(furan-2-ylmethyl)-5-(4-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)-1-(thiophen-2-yl)ethanone
-
2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid
binding structure analysis
2-(6,9-dimethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)-1-(4-fluorophenyl)ethanone
-
-
2-benzyl-3-mercaptopropanoic acid
-
2-Guanidinoethylmercaptosuccinic acid
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
2-mercaptomethyl-5-guanidinopentanoic acid
3-(6-amino-5-chloropyridin-3-yl)-2-(selanylmethyl)propanoic acid
-
3-Phenylpropanoic acid
-
-
3-Phenylpropionic acid
-
-
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
-
5-aminopentanoic acid
-
-
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
binding structure analysis
5-guanidino-2-(mercaptomethyl)pentanoic acid
-
6-amino-n-hexanoic acid
-
-
6-guanidinohexanoic acid
-
-
7-amino-2-(selanylmethyl)heptanoic acid
-
7-amino-2-(sulfanylmethyl)heptanoic acid
-
7-amino-2-[(propanoylselanyl)methyl]heptanoic acid
-
aminobenzylsuccinic acid
-
-
antithrombomodulin antibody
-
-
-
Beta-phenylpropionic acid
-
-
Ca2+
-
1 mM, 36% inhibition
Co2+
-
hydrolysis of hippuryl-L-Arg
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
DL-guanidinoethylmercaptosuccinic acid
-
-
DL-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
epsilon-aminocaproic acid
-
-
Guanidinoethylmercaptosuccinic acid
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
leech carboxypeptidase inhibitor
-
lipopolysaccharide
-
lipopolysaccharide treatment significantly decreases carboxypeptidase B activity. Administration of 5,5-dimethyl-1-pyrroline N-oxide to LPS-treated mice alleviates this loss of enzyme activity
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
-
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
-
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
-
methyl N-[[(1R,2S)-2-([N-[(benzyloxy)carbonyl]-beta-alanyl]amino)cyclobutyl]carbonyl]-beta-alaninate
-
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
-
Mg2+
-
1 mM, 24% inhibition
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
N-(3-chlorophenyl)-4-((5-(3-methoxybenzylthio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
-
N-[[di(propan-2-yl)amino]-[3-(4-methoxyphenyl)-2-trimethylsilyloxiran-2-yl]phosphinothioyl]-N-propan-2-ylpropan-2-amine
-
potato carboxypeptidase inhibitor
-
tick carboxypeptidase inhibitor
-
1,10-phenanthroline
-
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
-
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
-
2-Guanidinoethylmercaptosuccinic acid
-
2-Guanidinoethylmercaptosuccinic acid
-
-
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
-
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
-
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
-
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
-
2-mercaptomethyl-5-guanidinopentanoic acid
-
-
2-mercaptomethyl-5-guanidinopentanoic acid
-
-
2-mercaptomethyl-5-guanidinopentanoic acid
-
-
2-mercaptomethyl-5-guanidinopentanoic acid
-
-
6-aminohexanoic acid
-
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
binding structure analysis
DL-benzylsuccinic acid
-
-
DL-benzylsuccinic acid
-
-
EDTA
-
1 mM, 6 h, 90% loss of activity
EDTA
-
6 h, 1 mM, 90% inhibition
Guanidinoethylmercaptosuccinic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
Hg2+
-
1 mM, 97% inhibition
Hg2+
-
1 mM, 90% inhibition
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
leech carboxypeptidase inhibitor
-
-
-
leech carboxypeptidase inhibitor
-
-
-
leech carboxypeptidase inhibitor
-
-
-
leech carboxypeptidase inhibitor
-
-
-
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
Mn2+
-
inhibits activity
Mn2+
-
1 mM, 51% inhibition
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
-
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
-
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
-
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
recombinant protein
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
-
-
tick carboxypeptidase inhibitor
-
TCI, from the ixodid tick Rhipicephalus bursa, recombinant expression in Escherichia coli, DNA and amino acid sequence determination and analysis, binding structure and inhibition mechanism, overview
-
tick carboxypeptidase inhibitor
TCI, from Rhipicephalus bursa, recombinantly expressd in Escherichia coli strain BL21(DE3) periplasm and purification by cation exchange and adsorption chromatography, binding structure at the active site, overview
-
additional information
-
the enzyme is down-regulates upon feeding, the enzyme expression in the midgut is affected by ingestion of Plasmodium falciparum
-
additional information
no or poor inhibition of the enzyme by potato carboxypeptidase inhibitor, dependent on the pH, in contrast to other carboxypeptidases in the gut
-
additional information
-
no or poor inhibition of the enzyme by potato carboxypeptidase inhibitor, dependent on the pH, in contrast to other carboxypeptidases in the gut
-
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0.000002
(2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
pH 7.4, 22°C
0.000206
(S)-5-amino-2-((1-propyl-1H-imidazol-4-yl)methyl)pentanoic acid
-
0.001 - 0.0075
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
0.000007
2-(2-chloro-5-guanidinophenyl)-3-mercaptopropanoic acid
-
0.000034 - 0.004
2-(2-guanidinoethylthio)succinic acid
0.000002
2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
0.000007
2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid
pH 7.4, 22°C
0.009
2-(6,9-dimethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)-1-(4-fluorophenyl)ethanone
-
pH 7.5
0.163
2-benzyl-3-mercaptopropanoic acid
-
0.00005
2-Guanidinoethylmercaptosuccinic acid
-
pH 7.4
0.0014
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
pH 7.5
0.000002
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
pH 7.4, 22°C
0.00000042
5-guanidino-2-(mercaptomethyl)pentanoic acid
-
0.0000082 - 0.000063
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
0.01 - 0.0119
DL-benzylsuccinic acid
0.0011
DL-guanidinoethylmercaptosuccinic acid
-
pH 7.5
0.9
epsilon-aminocaproic acid
-
pH 7.4
0.0074 - 0.0361
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
0.275
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22°C
0.07
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22°C
0.0049 - 0.0416
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
0.41
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
pH 7.5, 22°C
0.165
methyl N-[[(1R,2S)-2-([N-[(benzyloxy)carbonyl]-beta-alanyl]amino)cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.4
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.5
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
pH 7.5, 22°C
0.0012 - 0.0036
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
0.0012
N-(3-chlorophenyl)-4-((5-(3-methoxybenzylthio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
0.0012 - 0.0045
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
0.043
N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.003
N-[[di(propan-2-yl)amino]-[3-(4-methoxyphenyl)-2-trimethylsilyloxiran-2-yl]phosphinothioyl]-N-propan-2-ylpropan-2-amine
-
0.000001 - 0.0000018
potato carboxypeptidase inhibitor
-
0.01
protamine
-
above, pH 7.4
0.0000013
tick carboxypeptidase inhibitor
-
pH 7.4, 23°C
-
additional information
additional information
-
0.001
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
pH 7.5
0.0075
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
pH 7.5
0.000034
2-(2-guanidinoethylthio)succinic acid
-
0.004
2-(2-guanidinoethylthio)succinic acid
-
0.0000082
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
pH 7.4
0.000063
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
pH 7.4, 22°C
0.01
DL-benzylsuccinic acid
-
pH 7.5
0.0119
DL-benzylsuccinic acid
-
pH 7.5
0.0074
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.0361
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.0049
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.0416
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.0012
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
pH 7.5
0.0036
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
pH 7.5
0.0012
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
pH 7.5
0.0045
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
pH 7.5
0.000001
potato carboxypeptidase inhibitor
-
pH 7.4
-
0.0000018
potato carboxypeptidase inhibitor
-
pH 7.4, 23°C
-
additional information
additional information
-
the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range
-
additional information
additional information
-
the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range
-
additional information
additional information
-
the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range
-
additional information
additional information
-
the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range
-
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Sakharov, D.V.; Plow, E.F.; Rijken, D.C.
On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
J. Biol. Chem.
272
14477-14482
1997
Homo sapiens
brenda
Eaton, D.L.; Malloy, B.E.; Tsai, S.P.; Henzel, W.; Drayna, D.
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
J. Biol. Chem.
266
21833-21838
1991
Homo sapiens
brenda
Hajjou, M.; Smine, A.; Guerard, F.; le Gal, Y.
Purification and some properties of a carboxypeptidase B from dogfish Scyliorhinus canicula
Comp. Biochem. Physiol. B
110
791-798
1995
Scyliorhinus canicula
-
brenda
Gates, B.J.; Travis, J.
Purification and characterization of carboxypeptidases A and B from the white shrimp (Penaeus setiferus)
Biochemistry
12
1867-1874
1973
Penaeus setiferus
brenda
Reeck, G.R.; Walsh, K.A.; Neurath, H.
Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice
Biochemistry
10
4690-4698
1971
Bos taurus
brenda
Clauser, E.; Gardell, S.J.; Craik, C.S.; MacDonald, R.J.; Rutter, W.J.
Structural characterization of the rat carboxypeptidase A1 and B genes. Comparative analysis of the rat carboxypeptidase gene family
J. Biol. Chem.
263
17837-17845
1988
Rattus norvegicus
brenda
Sokolovsky, M.
Affinity chromatography of carboxypeptidase B
Methods Enzymol.
34
411-414
1974
Bos taurus
brenda
Folk, J.E.
Carboxypeptidase B (porcine pancreas)
Methods Enzymol.
19
504-508
1970
Bos taurus
-
brenda
Folk, J.E.; Piez, K.A.; Carroll, W.R.; Gladner, J.A.
Carboxypeptidase B
J. Biol. Chem.
235
2272-2277
1960
Sus scrofa
brenda
Wintersberger, E.; Cox, D.J.; Neurath, H.
Bovine pancreatic procarboxypeptidase B. I. Isolation, properties, and activation
Biochemistry
1
1069-1078
1962
Bos taurus
brenda
Prahl, J.W.; Neurath, H.
Pancreatic enzymes of the spiny pacific dogfish. II. Procarboxypeptidase B and carboxypeptidase B
Biochemistry
5
4137-4145
1966
Squalus acanthias
-
brenda
Geokas, M.C.; Largman, C.; Brodrick, J.W.; Raeburn, S.; Rinderknecht, H.
Human pancreatic carboxypeptidase B. I. Isolation, purification, and characterization of fraction II
Biochim. Biophys. Acta
391
396-402
1975
Homo sapiens
brenda
Brodrick, J.W.; Geokas, M.C.; Largman, C.
Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion
Biochim. Biophys. Acta
452
468-481
1976
Homo sapiens
brenda
Marinkovic, D.V.; Marinkovic, J.N.; Erds, E.G.; Robinson, C.J.G.
Purification of carboxypeptidase B from human pancreas
Biochem. J.
163
253-260
1977
Homo sapiens
brenda
Alter, G.M.M.; Leussing, D.L.; Neurath, H.; Vallee, B.L.
Kinetic properties of carboxypeptidase B in solutions and crystals
Biochemistry
16
3663-3668
1977
Bos taurus
brenda
Prins, R.A.; van Rheenen, D.L.; van't Klooster, A.T.
Characterization of microbial proteolytic enzymes in the rumen
Antonie van Leeuwenhoek
49
585-595
1983
rumen bacterium
brenda
Bown, D.P.; Wilkinson, H.S.; Gatehouse, J.A.
Midgut carboxypeptidase from Helicoverpa armigera (Lepidoptera: Noctuidae) larvae: enzyme characterisation, cDNA cloning and expression
Insect Biochem. Mol. Biol.
28
739-749
1998
Helicoverpa armigera
brenda
Sdi, P.; Dala, E.; Szajani, B.
Preparation, characterization, and application of a novel immobilized carboxypeptidase B
Appl. Biochem. Biotechnol.
22
31-43
1989
Sus scrofa
brenda
Hass, G.M.; Derr, J.E.; Makus, D.J.; Ryan, C.A.
Purification and characterization of the carboxypeptidase isoinhibitors from potatoes
Plant Physiol.
64
1022-1028
1979
Bos taurus
brenda
Sasaki, I.; Gotoh, H.; Yamamoto, R.; Hasegawa, H.; Yamashita, J.; Horio, T.
Hydrophobic-ionic chromatography. Its application to purification of porcine pancreas enzymes
J. Biochem.
86
1537-1548
1979
Sus scrofa
brenda
Ferrell, R.E.; Camacho, Z.; Kitto, G.B.
Purification of a carboxypeptidase B-like enzyme from the starfish Dermasterias imbricata
Biochim. Biophys. Acta
386
260-269
1975
Dermasterias imbricata
brenda
Neurath, H.
Carboxypeptidase A and B
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
4
11-36
1960
Bos taurus
-
brenda
Reeck, G.R.; Neurath, H.
Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish
Biochemistry
11
3947-3955
1972
Protopterus aethiopicus
brenda
Valnickova, Z.; Thogersen, I.B.; Christensen, S.; Chu, C.T.; Pizzo, S.V.; Enghild, J.J.
Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein
J. Biol. Chem.
371
12937-12943
1996
Homo sapiens
brenda
Marquez-Mendez, M.
Purification of carboxypeptidase B by metal chelation affinity chromatography
J. Biochem. Biophys. Methods
24
51-61
1992
Nephrops norvegicus
brenda
Bradley, G.; Naude, R.J.; Muramoto, K.; Yamauchi, F.; Oelofsen, W.
Ostrich (Struthio camelus) carboxypeptidase B: purification, kinetic properties and characterization of the pancreatic enzyme
Int. J. Biochem. Cell Biol.
28
521-529
1996
Struthio camelus, Sus scrofa
brenda
Ortego, F.; Novillo, C.; Castanera, P.
Characterization and distribution of digestive proteases of the stalk corn borer, Sesamia nonagrioides Lef. (Lepidoptera: noctuidae)
Arch. Insect Biochem. Physiol.
32
163-180
1996
Sesamia nonagrioides, Sesamia nonagrioides Lef.
-
brenda
Edge, M.; Forder, C.; Hennam, J.; Lee, I.; Tonge, D.; Hardern, I.; Fitton, J.; Eckersley, K.; East, S.; Shufflebotham, A.; Blakey, D.; Slater, A.
Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants
Protein Eng.
11
1229-1234
1998
Homo sapiens
brenda
Mao, S.S.; Colussi, D.; Bailey, C.M.; Bosserman, M.; Burlein, C.; Gardell, S.J.; Carroll, S.S.
Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor
Anal. Biochem.
319
159-170
2003
Homo sapiens
brenda
Kishimura, H.; Hayashi, K.
Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis
Comp. Biochem. Physiol. B
133
183-189
2002
Asterias amurensis
brenda
Matsumoto, A.; Motozaki, K.; Seki, T.; Sasaki, R.; Kawabe, T.
Expression of human brain carboxypeptidase B, a possible cleaving enzyme for beta-amyloid precursor protein, in peripheral fluids
Neurosci. Res.
39
313-317
2001
Homo sapiens
brenda
Ladisch, M.R.; Kohlmann, K.L.
Recombinant human insulin
Biotechnol. Prog.
8
469-478
1992
Sus scrofa
brenda
Adler, M.; Bryant, J.; Buckman, B.; Islam, I.; Larsen, B.; Finster, S.; Kent, L.; May, K.; Mohan, R.; Yuan, S.; Whitlow, M.
Crystal structures of potent thiol-based inhibitors bound to carboxypeptidase B
Biochemistry
44
9339-9347
2005
Sus scrofa (P09955), Sus scrofa
brenda
Kishimura, H.; Hayashi, K.; Ando, S.
Characteristics of carboxypeptidase B from pyloric ceca of the starfish Asterina pectinifera
Food Chem.
95
264-269
2005
Patiria pectinifera
-
brenda
Aviles, F.X.; Vendrell, J.
Carboxypeptidase B
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press
2
831-833
2004
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
-
brenda
Wang, P.; Li, G.; Kain, W.
Characterization and cDNA cloning of midgut carboxypeptidases from Trichoplusia ni
Insect Biochem. Mol. Biol.
34
831-843
2004
Trichoplusia ni
brenda
Bayes, A.; de la Vega, M.R.; Vendrell, J.; Aviles, F.X.; Jongsma, M.A.; Beekwilder, J.
Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B
Insect Biochem. Mol. Biol.
36
654-664
2006
Helicoverpa zea (Q3T905), Helicoverpa zea
brenda
Lavazec, C.; Bonnet, S.; Thiery, I.; Boisson, B.; Bourgouin, C.
cpbAg1 encodes an active carboxypeptidase B expressed in the midgut of Anopheles gambiae
Insect Mol. Biol.
14
163-174
2005
Anopheles gambiae
brenda
Arolas, J.L.; Lorenzo, J.; Rovira, A.; Castella, J.; Aviles, F.X.; Sommerhoff, C.P.
A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization
J. Biol. Chem.
280
3441-3448
2005
Homo sapiens
brenda
Arolas, J.L.; Popowicz, G.M.; Lorenzo, J.; Sommerhoff, C.P.; Huber, R.; Aviles, F.X.; Holak, T.A.
The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
J. Mol. Biol.
350
489-498
2005
Homo sapiens (P15086), Homo sapiens
brenda
Borgstroem, A.; Regner, S.
Active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
Pancreatology
5
530-536
2005
Homo sapiens
brenda
Higuchi, T.; Nakamura, T.; Kakutani, H.; Ishii, H.
Thrombomodulin suppresses invasiveness of HT1080 tumor cells by reducing plasminogen activation on the cell surface through activation of thrombin-activatable fibrinolysis inhibitor
Biol. Pharm. Bull.
32
179-185
2009
Homo sapiens
brenda
Luo, X.; Bathgate, R.A.; Zhang, W.J.; Liu, Y.L.; Shao, X.X.; Wade, J.D.; Guo, Z.Y.
Design and recombinant expression of insulin-like peptide 5 precursors and the preparation of mature human INSL5
Amino Acids
39
1343-1352
2010
Homo sapiens
brenda
Sharif, S.A.; Du, X.; Myles, T.; Song, J.J.; Price, E.; Lee, D.M.; Goodman, S.B.; Nagashima, M.; Morser, J.; Robinson, W.H.; Leung, L.L.
Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis
Arthritis Rheum.
60
2902-2912
2009
Homo sapiens
brenda
Fernandez, D.; Pallares, I.; Vendrell, J.; Aviles, F.X.
Progress in metallocarboxypeptidases and their small molecular weight inhibitors
Biochimie
92
484-500
2010
Sus scrofa (P09955)
brenda
Fernandez, D.; Torres, E.; Aviles, F.X.; Ortuno, R.M.; Vendrell, J.
Cyclobutane-containing peptides: evaluation as novel metallocarboxypeptidase inhibitors and modelling of their mode of action
Bioorg. Med. Chem.
17
3824-3828
2009
Homo sapiens
brenda
Jiang, L.P.; Zou, C.; Yuan, X.; Luo, W.; Wen, Y.; Chen, Y.
N-terminal modification increases the stability of the recombinant human endostatin in vitro
Biotechnol. Appl. Biochem.
54
113-120
2009
Homo sapiens
brenda
Son, Y.J.; Kim, C.K.; Kim, Y.B.; Kweon, D.H.; Park, Y.C.; Seo, J.H.
Effects of citraconylation on enzymatic modification of human proinsulin using trypsin and carboxypeptidase B
Biotechnol. Prog.
25
1064-1070
2009
Sus scrofa
brenda
Fernandez, D.; Aviles, F.X.; Vendrell, J.
A new type of five-membered heterocyclic inhibitors of basic metallocarboxypeptidases
Eur. J. Med. Chem.
44
3266-3271
2009
Helicoverpa zea, Homo sapiens
brenda
Luo, X.; Bathgate, R.A.; Liu, Y.L.; Shao, X.X.; Wade, J.D.; Guo, Z.Y.
Recombinant expression of an insulin-like peptide 3 (INSL3) precursor and its enzymatic conversion to mature human INSL3
FEBS J.
276
5203-5211
2009
Sus scrofa
brenda
Chatterjee, S.; Ehrenshaft, M.; Bhattacharjee, S.; Deterding, L.; Bonini, M.; Corbett, J.; Kadiiska, M.; Tomer, K.; Mason, R.
Immuno-spin trapping of a post-translational carboxypeptidase B1 radical formed by a dual role of xanthine oxidase and endothelial nitric oxide synthase in acute septic mice
Free Radic. Biol. Med.
46
454-461
2009
Mus musculus
brenda
Rider, S.A.; Davies, S.J.; Jha, A.N.; Clough, R.; Sweetman, J.W.
Bioavailability of co-supplemented organic and inorganic zinc and selenium sources in a white fishmeal-based rainbow trout (Oncorhynchus mykiss) diet
J. Anim. Physiol. Anim. Nutr. (Berl.)
94
99-110
2010
Oncorhynchus mykiss
brenda
Chatterjee, S.; Lardinois, O.; Bonini, M.G.; Bhattacharjee, S.; Stadler, K.; Corbett, J.; Deterding, L.J.; Tomer, K.B.; Kadiiska, M.; Mason, R.P.
Site-specific carboxypeptidase B1 tyrosine nitration and pathophysiological implications following its physical association with nitric oxide synthase-3 in experimental sepsis
J. Immunol.
183
4055-4066
2009
Mus musculus, Sus scrofa
brenda
Toth, S.I.; Smith, L.A.; Ahmed, S.A.
Extreme sensitivity of botulinum neurotoxin domains towards mild agitation
J. Pharm. Sci.
98
3302-3311
2009
Sus scrofa (P09955)
brenda
Lepus, C.; Song, J.; Wang, Q.; Wagner, C.; Lindstrom, T.; Chu, C.; Sokolove, J.; Leung, L.; Robinson, W.
Carboxypeptidase B serves as a protective mediator in osteoarthritis
Arthritis Rheum.
66
101-106
2014
Homo sapiens, Mus musculus
brenda
Raz, A.; Dinparast Djadid, N.; Zakeri, S.
Molecular characterization of the carboxypeptidase B1 of Anopheles stephensi and its evaluation as a target for transmission-blocking vaccines
Infect. Immun.
81
2206-2216
2013
Anopheles stephensi (F1ALX3), Anopheles stephensi
brenda
Ktari, N.; Ben Khaled, H.; Lassoued, I.; Ghorbel, S.; Nasri, M.
Isolation and characteristics of carboxypeptidase B from zebra blenny (Salaria basilisca) viscera
J. Aquatic Food Product Technol.
23
208-220
2014
Salaria basilisca
-
brenda
Yoshimoto, N.; Itoh, T.; Inaba, Y.; Ishii, H.; Yamamoto, K.
Structural basis for inhibition of carboxypeptidase B by selenium-containing inhibitor: selenium coordinates to zinc in enzyme
J. Med. Chem.
56
7527-7535
2013
Sus scrofa (P09955), Sus scrofa
brenda
Kovacs, A.; Szabo, L.; Longstaff, C.; Tenekedjiev, K.; Machovich, R.; Kolev, K.
Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin
Thromb. Res.
133
80-87
2014
Sus scrofa
brenda
Akparov, V.; Sokolenko, N.; Timofeev, V.; Kuranova, I.
Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine
Acta Crystallogr. Sect. F
71
1335-1340
2015
Sus scrofa (P09955), Sus scrofa
brenda
Kim, D.G.; Kim, H.J.; Kim, H.J.
Effects of carboxypeptidase B treatment and elevated temperature on recombinant monoclonal antibody charge variants in cation-exchange chromatography analysis
Arch. Pharm. Res.
39
1472-1481
2016
Rattus norvegicus
brenda
Akparov, V.; Timofeev, V.; Maghsoudi, N.; Kuranova, I.
Three-dimensional structure of porcine pancreatic carboxypeptidase B with an acetate ion and two zinc atoms in the active site
Crystallogr. Rep.
62
249-253
2017
Sus scrofa (P09955)
-
brenda
Akparov, V.; Timofeev, V.; Khaliullin, I.; Svedas, V.; Kuranova, I.
Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific substrate
J. Biomol. Struct. Dyn.
36
956-965
2018
Sus scrofa (P09955)
brenda
Leung, L.L.K.; Morser, J.
Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity
J. Thromb. Haemost.
16
1474-1486
2018
Mus musculus
brenda