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Information on EC 3.4.17.2 - carboxypeptidase B
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EC Tree
3.4.17.2 carboxypeptidase BSpecify your search results
Word Map
- 3.4.17.2
-
cardiopulmonary
- cardiac
- artery
-
postoperative
- coronary
- aortic
-
perioperative
- myocardial
- pulmonary
- ventricular
-
hemodynamic
- heparin
-
transfusion
-
elective
-
circuit
-
intraoperative
- valve
-
bleeding
-
hypothermic
-
anesthesia
- venous
-
extracorporeal
-
ventilation
- protamine
-
inotropic
-
cardioplegia
-
sternotomy
-
rewarming
-
hemodilution
-
revascularization
-
cross-clamping
- atrial
-
normothermic
-
wean
-
hematocrit
-
circulatory
-
off-pump
- analysis
-
cardiothoracic
- synthesis
-
intra-aortic
- medicine
-
open-heart
-
thoracotomy
-
in-hospital
- drug development
-
extubation
- pharmacology
- crystalloid
-
cannulation
-
roller
-
transesophageal
-
fentanyl
-
antegrade
-
reoperation
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cpb, carboxypeptidase b, basic carboxypeptidase, pancreas-specific protein, carboxypeptidase b1, b carboxypeptidase, ppcpb, hbcpb, cpbag1, cpbas1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
47 kDa zymogen granule membrane associated protein
-
-
-
-
basic carboxypeptidase
carboxypeptidase B
Carboxypeptidase B1
carboxypeptidase BII
-
-
-
-
CPB
EC 3.4.12.3
-
-
formerly
-
EC 3.4.2.2
-
-
formerly
-
Pancreas-specific protein
-
-
-
-
PASP
-
-
-
-
protaminase
thrombin-activatable fibrinolysis inhibitor
tissue carboxypeptidase B
ZAP47
-
-
-
-
additional information
CPB
-
-
-
-
protaminase
-
-
-
-
thrombin-activatable fibrinolysis inhibitor
-
possesses carboxypeptidase B-like activity
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential release of a C-terminal lysine or arginine amino acid
-
-
-
-
preferential release of a C-terminal lysine or arginine amino acid
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
preferential release of a C-terminal lysine or arginine amino acid
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
preferential release of a C-terminal lysine or arginine amino acid
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
preferential release of a C-terminal lysine or arginine amino acid
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-24-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(2-furyl)acryloyl-L-Ala-L-Arg + H2O
3-(2-furyl)acryloyl-L-Ala + L-Arg
-
-
-
?
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR + H2O
biotin-(epsilon-aminocaproic acid)2-GLMVGGVV + Arg
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
-
mutant enzymes S253K and S253R are inactive
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
-
129% of the activity with hippuryl-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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Fibrin + H2O
?
-
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA
-
-
?
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
-
-
?
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
-
-
?
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 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 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
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
Co2+
Zinc
Zn2+
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
(S)-2-(2-((S)-1-carboxy-2-(1H-imidazol-5-yl)ethylamino)ethylamino)-5-guanidinopentanoic acid
IC50: 17 microgram/ml
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
-
-
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
-
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
binding structure analysis
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 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
-
-
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-[[(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
-
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
binding structure analysis
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
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
-
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
allopurinol
-
addition of allopurinol alone and allopurinol plus 5,5-dimethyl-1-pyrroline N-oxide results in increased CPB1 activity
Thrombomodulin
-
HT1080 cells mediate activation of TAFI in plasma in the presence of soluble-type thrombomodulin through cell-dependent prothrombin activation. HT1080 cells stably expressing thrombomodulin mediate plasma TAFI activation without added soluble thrombomodulin
-
additional information
-
the enzyme expression in the midgut is affected by ingestion of Plasmodium falciparum
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values of mutant enzymes with hippuryl-Glu as substrate
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000002
(2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
pH 7.4, 22°C
0.001 - 0.0075
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
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
0.0014
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
pH 7.5
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
0.41
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
-
0.043
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
-
0.001
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
0.000063
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
pH 7.4, 22°C
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
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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000055
(2S)-7-amino-2-[(hydroxy[(1R)-2-methyl-1-[(3-phenylpropanoyl)amino]propyl]phosphoryl)methyl]heptanoic acid
Sus scrofa
pH and temperature not specified in the publication
0.000024
2-(4-(furan-2-ylmethyl)-5-(4-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)-1-(thiophen-2-yl)ethanone
Sus scrofa
-
0.000000025
3-(6-amino-5-chloropyridin-3-yl)-2-(selanylmethyl)propanoic acid
Sus scrofa
pH and temperature not specified in the publication
0.000002
7-amino-2-(selanylmethyl)heptanoic acid
Sus scrofa
pH and temperature not specified in the publication
0.000034
7-amino-2-(sulfanylmethyl)heptanoic acid
Sus scrofa
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
electrochemiluminescence assay. Development of a highly sensitive method for measurement of basic carboxypeptidase activity. The assay format depends on the recognition of a C-terminal carboxylic acid residue of a peptide with the C-terminal sequence GGVV by the monoclonal antibody, G2-10. Removal of the masking C-terminal Arg by a basic carboxypeptidase exposes the recognition site for the antibody. High sensitivity, detection limits of 1-2 pM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5 - 7.8
7.5 - 8
7.65
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
pH 5.5: about 60% of maximal activity, pH 9.0: about 30% of maximal activity
6 - 10
-
pH 6: about 60% of maximal activity with carboxypeptidase B I, about 50% of maximal activity with carboxypeptidase B II, pH 10: about 70% of maximal activity with carboxypeptidase B I, about 60% of maximal activity with carboxypeptidase B II, cleavage of hippuryl-L-Arg
6 - 9
-
about 40% of maximal activity at pH 6 and 9, soluble enzyme and immobilized enzyme
7 - 10.5
-
pH 7: about 45% of maximal activity with carboxypeptidase B I, about 30% of maximal activity with carboxypeptidase B II, pH: 10.5: about 90% of maximal activity with carboxypeptidase B I, about 80% of maximal activity with carboxypeptidase B II, hydrolysis of hippuryl-L-Arg
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
55
additional information
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
35 - 65
-
35°C: 45% of maximal activity, 65°C: about 50% of maximal activity, immobilized enzyme
45 - 80
-
45°C: about 35% of maximal activity, 80°C: about 60% of maximal activity
30 - 70
-
30°C: about 40% of maximal activity, 70°C: about 55% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in synovial fluids from osteoarthritis patients, high levels of proCPB are associated with high levels of proinflammatory cytokines and complement components, and levels of proCPB correlated positively with those of membrane attack complex (MAC)
brenda
-
carboxypeptidase B from pancreatic tissue, carboxypeptidase B I and B II from pancreatic juice. Carboxypeptidase B is converted to carboxypeptidase B II by trypsin
brenda
-
the activated carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein
brenda
-
confocal microscopy results indicate that levels of both CPB1 and nitric oxide synthase-3 are high in the septic spleen and that CPB1 colocalizes with nitric oxide synthase-3 in the sinus-lining cells of the red pulp. LPS treatment results in the translocation of nitric oxide synthase-3 to the cytosol and colocalization with CPB1
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
confocal microscopy results indicate that levels of both CPB1 and nitric oxide synthase-3 are high in the septic spleen and that CPB1 colocalizes with nitric oxide synthase-3 in the sinus-lining cells of the red pulp. LPS treatment results in the translocation of nitric oxide synthase-3 to the cytosol and colocalization with CPB1
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
anti-CPBAs1 directed antibodies can significantly reduce the mosquito infection rate in the test group compared with the control group
malfunction
-
Cpb2 knockout mice develop greater cartilage damage than wild-type mice and have a greater number of osteophytes and degree of synovitis
malfunction
-
Cpb2 knockout mice develop greater cartilage damage than wild-type mice and have a greater number of osteophytes and degree of synovitis
malfunction
-
among mice genetically deficient in either carboxypeptidase B2 (Cpb2) or carboxypeptidase N (Cpn), in a model of hemolytic-uremic syndrome, Cpb2-/- mice have the worst disease, followed by Cpn-/- mice, with wild-type mice being the most protected. This model is driven by C5a, and shows that carboxypeptidase B2 is important in inactivating C5a. Cpn-/- mice are generated by disruption of Cpn1. When mice are challenged acutely with cobra venom factor, the reverse phenotype is observed. Cpn-/- mice have markedly worse disease than Cpb2-/- mice, and wild-type mice are resistant
metabolism
-
nitrone spin-trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) and a combination of immuno-spin trapping and mass spectrometry is used to identify in vivo products of radical reactions in mice. Dose-dependent production of 5,5-dimethyl-1-pyrroline N-oxide-CPB1 adducts are detected in the spleens of mice treated with lipopolysaccharide and also under normal physiological conditions. Treatments with inhibitors and experiments with knock-out mice indicate that xanthine oxidase and endothelial nitric oxide synthase are important sources of the reactive species that lead to CPB1 adduct formation
metabolism
-
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA but conversely, CPB and plasmin together can stimulate fibrinolysis
physiological function
-
carboxypeptidase B activity is not affected by Zn supplementation
physiological function
in contrast to botulinum neurotoxin carboxypeptidase is not affected by mechanical stirring
physiological function
-
thrombin-activatable CPB plays a central homeostatic role in rheumatoid arthritis by regulating neutrophil viability and reducing synoviocyte adhesion
physiological function
-
thrombomodulin suppresses pericellular fibrinolysis and plasma-induced tumor cell invasion, which is mediated by plasma TAFI activation
physiological function
-
the enzyme delays fibrinolysis. CPB2 is important in inactivating C5a
physiological function
-
the enzyme removes C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CBPB1_BOVIN
417
0
47348
Swiss-Prot
Secretory Pathway (Reliability: 3)
CBPB1_CANLF
416
0
47597
Swiss-Prot
Secretory Pathway (Reliability: 2)
CBPB1_HUMAN
417
0
47368
Swiss-Prot
Secretory Pathway (Reliability: 2)
CBPB1_PIG
416
0
47381
Swiss-Prot
Secretory Pathway (Reliability: 2)
CBPB1_RAT
415
0
47515
Swiss-Prot
Secretory Pathway (Reliability: 2)
CBPB_ASTAS
303
0
33918
Swiss-Prot
other Location (Reliability: 1)
CBPB_HELZE
429
0
48393
Swiss-Prot
Secretory Pathway (Reliability: 2)
CBPB_PROAT
15
0
1749
Swiss-Prot
other Location (Reliability: 1)
B7P4Y5_IXOSC
386
0
43516
TrEMBL
other Location (Reliability: 1)
G0QP71_ICHMG
Ichthyophthirius multifiliis (strain G5)
284
0
33602
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0D5BXE7_GIAIN
143
0
16039
TrEMBL
other Location (Reliability: 3)
E0VDV1_PEDHC
428
0
47698
TrEMBL
other Location (Reliability: 1)
Q6J660_AEDPO
412
0
45628
TrEMBL
Secretory Pathway (Reliability: 1)
Q6J659_OCHTR
411
0
45704
TrEMBL
Secretory Pathway (Reliability: 1)
E0W0X1_PEDHC
383
0
44419
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3G4RHX0_GIAIN
123
0
14123
TrEMBL
other Location (Reliability: 2)
G0QP77_ICHMG
Ichthyophthirius multifiliis (strain G5)
260
0
30296
TrEMBL
other Location (Reliability: 2)
A0A8M1NG52_DANRE
265
0
29803
TrEMBL
other Location (Reliability: 3)
B6AFX8_CRYMR
Cryptosporidium muris (strain RN66)
755
1
85778
TrEMBL
Secretory Pathway (Reliability: 3)
Q6J658_9DIPT
411
0
45792
TrEMBL
Secretory Pathway (Reliability: 2)
S5YTW2_GIAIN
161
0
18180
TrEMBL
other Location (Reliability: 1)
Q6J661_AEDAE
412
0
45814
TrEMBL
Secretory Pathway (Reliability: 2)
Q6J6D1_AEDAE
425
1
48150
TrEMBL
Secretory Pathway (Reliability: 1)
A0A023U939_GIAIN
160
0
18051
TrEMBL
other Location (Reliability: 2)
G0QKJ1_ICHMG
Ichthyophthirius multifiliis (strain G5)
261
0
30603
TrEMBL
other Location (Reliability: 2)
B7QLQ3_IXOSC
438
0
48818
TrEMBL
other Location (Reliability: 3)
A0A8B6HHF7_MYTGA
325
1
36407
TrEMBL
Secretory Pathway (Reliability: 2)
A0A059SRL3_GIAIN
149
0
16697
TrEMBL
other Location (Reliability: 2)
A0A8M1P961_DANRE
416
0
46670
TrEMBL
Secretory Pathway (Reliability: 1)
Q6J6D2_AEDAE
412
0
46157
TrEMBL
Secretory Pathway (Reliability: 1)
E0V9S1_PEDHC
297
0
33471
TrEMBL
other Location (Reliability: 2)
A0A7T9KRE1_NILLU
371
0
41684
TrEMBL
other Location (Reliability: 3)
Q6MQZ5_BDEBA
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
308
0
33979
TrEMBL
-
A0A0N1FK38_9ACTN
357
0
39532
TrEMBL
-
A0A084GG21_PSEDA
707
0
77909
TrEMBL
Secretory Pathway (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23500
32000
34000
34300
35000
70000
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB, dimer formation, band immunoreactive to an antibody specific to 3-nitrotyrosine
9200
additional information
23500
-
x * 9200 + x * 23500, carboxypeptidase B I, SDS-PAGE after reduction with 2-mercaptoethanol
32000
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB
35000
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB
9200
-
x * 9200 + x * 23500, carboxypeptidase B I, SDS-PAGE after reduction with 2-mercaptoethanol
additional information
-
analysis of active enzyme and inactive proenzyme by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
dimer
-
x * 9200 + x * 23500, carboxypeptidase B I, SDS-PAGE after reduction with 2-mercaptoethanol
additional information
-
the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region
additional information
-
the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region
additional information
-
the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region
additional information
-
the pancreatic enzyme is divided in the activation domain, residues 1-80, and the enzyme domain, residues 96-401, linked by a connecting region, residues 81-95
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nitrosylation
proteolytic modification
nitrosylation
-
a post-translational DMPO-nitrone adduct formed with CPB1 in mice treated with a single bolus dose of lipopolysaccharide is detected
nitrosylation
-
LPS-induced septic shock produces tyrosine nitration in vivo which is due to the formation of peroxynitrite and is mediated by xanthine oxidase and nitric oxide synthase-3. Nitrosylation leads to the inactivation of the enzyme
nitrosylation
-
peroxynitrite-dependent tyrosine nitration leading to inactivation of the enzyme. At least 11 peptides with five sites of nitration on tyrosine residues are identified. These include Tyr92, Tyr210, Tyr277, Tyr248, and Tyr198. Of these, Tyr248 and Tyr198 are located in the catalytic site of CPB
proteolytic modification
-
the enzyme contains a propeptide and a signal peptide
proteolytic modification
-
the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin
proteolytic modification
-
40000 Da prepro form of the enzyme, 30000 Da mature enzyme form
proteolytic modification
cleavage and activation of the recombinant zymogen by trypsin
proteolytic modification
-
the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin
proteolytic modification
-
zymogen activation by trypsin cleaving the activation peptide off the proenzyme at room temperature and pH 8.2
proteolytic modification
-
the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin
proteolytic modification
-
procarboxypeptidase B has a MW of 44500 Da, activation by bovine trypsin yields carboxypeptidase B
proteolytic modification
-
the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme in complex with tick carboxypeptidase inhibitor, sitting drop vapour diffusion method, mixing of equal volumes of protein and reservoir solutions, the latter containing 0.1 M bis-Tris. pH 5.5, 0.2 M lithium sulfate monohydrate, and 25% w/v PEG 3350, a few weeks at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
crystal structures of selenium-, sulfur-, and phosphinic acid containing inhibitors bound to porcine pancreatic carboxypeptidase B are determined at 1.7, 2.15 and 1.9 A, respectively
crystals of porcine pancreatic carboxypeptidase B are grown by the capillary counter-diffusion method in the presence of polyethylene glycol and zinc acetate. The three-dimensional structure of carboxypeptidase B is determined at 1.40 A resolution. The structure contains five zinc atoms, two of which are present in the active site of the enzyme, and an acetate ion
crystals of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine are grown in a capillary in microgravity using the counter-diffusion technique. Crystals are grown in a form belonging to the same space group, P4(1)2(1)2, as the uncomplexed enzyme. X-ray data are collected to a resolution of 1.25 A
enzyme in complex with inhibitors DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, 2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid, (2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid, or 5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid, hanging drop vapour diffusion method, 0.21 mg/ml protein in 10 mM Tris, pH 7.0, 1 mM inhibitor, and 50 mM NaCl, mixed with an equal volume of 0.002 ml of reservoir solution containing 0.15-0.30 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 12-22% PEG 8000, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
structure of the complex of the enzyme with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74 A. Crystals of the enzyme/N-sulfamoyl-L-phenylalanine complex are grown in a capillary in microgravity using the counter-diffusion technique
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D253K
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. Activity with hippuryl-Glu and hippuryl-Asp, this activity is reduced hundred-fold compared with the native enzyme with hippuryl-Arg as substrate
D253R
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. Activity with hippuryl-Glu and hippuryl-Asp, this activity is reduced hundred-fold compared with the native enzyme with hippuryl-Arg as substrate
G251T/D253K
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. 100times more active against hippuryl-L-Glu as substrate than the single mutant D253K
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 45
50
60
additional information
-
heat stability is markedly increased as an effect of immobilization
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of the commercial pancreatic preparation by hydrophobic interaction chromatography
native enzyme 418fold from pyloric ceca to near homogeneity by gel filtration, anion exchange chromatography, and another step of gel filtration
-
native proenzyme from pancreatic juice, separation of active enzyme and inactive proenzyme by gel filtration
-
purified by chromatography on Q-Sepharose Fast Flow, Heparin-Sepharose CL-6B, Sephacryl S-300, and plasminogen-Sepharose columns
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of midgut carboxypeptidase B
-
DNA and amino acid sequence determination and analysis, expression of the zymogen in Pichia pastoris
DNA sequence determination, phylogenetic tree
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decreased expression after blood-feeding in the non-infected group
expression level is increased after ingestion of the mature gametocytes of Plasmodium falciparum
in synovial fluids from osteoarthritis patients CPB expression is up-regulated
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
-
the enzyme is a serum marker for acute pancreatitis and pancreatic graft injection
drug development
the enzyme is a target for design of active site inhibitors based on the structure of tick carboxypeptidase inhibitor, a potential antithrombolytic drug
medicine
cpbAs1 can be introduced as a transmission-blocking vaccine candidate in regions where Anopheles stephensi is the main malaria vector
pharmacology
carboxypeptidase B is commonly used in the industrial insulin production and as a template for drug design
analysis
-
the immobilized carboxypeptidase B is used for stepwise digestion of cytochrome c
analysis
-
carboxypeptidase B treatment of recombinant monoclonal antibodies indicates that C-terminal lysine variants are present mainly among the basic species but also to some extent among the acidic species
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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