3.4.17.2: carboxypeptidase B
This is an abbreviated version!
For detailed information about carboxypeptidase B, go to the full flat file.
Word Map on EC 3.4.17.2
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3.4.17.2
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cardiopulmonary
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cardiac
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artery
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postoperative
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coronary
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aortic
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perioperative
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myocardial
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pulmonary
-
ventricular
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hemodynamic
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heparin
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transfusion
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elective
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circuit
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intraoperative
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valve
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bleeding
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hypothermic
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anesthesia
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venous
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extracorporeal
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ventilation
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protamine
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inotropic
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cardioplegia
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sternotomy
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rewarming
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hemodilution
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revascularization
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cross-clamping
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atrial
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normothermic
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wean
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hematocrit
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circulatory
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off-pump
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analysis
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cardiothoracic
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synthesis
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intra-aortic
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medicine
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open-heart
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thoracotomy
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in-hospital
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drug development
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extubation
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pharmacology
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crystalloid
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cannulation
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roller
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transesophageal
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fentanyl
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antegrade
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reoperation
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diagnostics
- 3.4.17.2
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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
Reaction
preferential release of a C-terminal lysine or arginine amino acid =
Synonyms
47 kDa zymogen granule membrane associated protein, aCAP, B carboxypeptidase, basic carboxypeptidase, carboxypeptidase B, Carboxypeptidase B1, carboxypeptidase B2, carboxypeptidase BII, Cbp, CPB, CPB1, CPB2, CPBAg1, cpbAs1, EC 3.4.12.3, EC 3.4.2.2, HBCPB, HzCPB, More, Pancreas-specific protein, PASP, PCB, PcpB, pp-CpB, ppCPB, protaminase, TAFI, thrombin-activatable fibrinolysis inhibitor, thrombin-activatable procarboxypeptidase B, tissue carboxypeptidase B, ZAP47
ECTree
3.4.17.2 carboxypeptidase BAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.17.2 - carboxypeptidase B
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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
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hydrolyzed by mutant enzyme D253K and mutant enzyme D253R, wild type enzyme shows no activity
-
-
?
hippuryl-L-Glu + H2O
hippuric acid + Glu
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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
?
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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 + ?
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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
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mutant enzymes S253K and S253R are inactive
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
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129% of the activity with hippuryl-L-Arg
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-
?
additional information
?
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hydrolysis of peptide bonds of Lys, Arg, Arn, homoarginine and S-(beta-aminoethyl)cysteine. Esterase activity towards carboxy terminal Arg
-
-
?
additional information
?
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-
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
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-
?
additional information
?
-
the enzyme is highly specific for excising C-terminal Lys from peptides and protein substrates
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-
?
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
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-
?
additional information
?
-
-
the enzyme plays a role in the fibrinolytic or coagulation system
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-
?
additional information
?
-
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mechanism for the antifibrinolytic affect of the plasma enzyme
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-
?
additional information
?
-
-
active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
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-
?
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
-
-
?
