Information on EC 3.4.17.2 - carboxypeptidase B

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
3.4.17.2
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase B
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
preferential release of a C-terminal lysine or arginine amino acid
show the reaction diagram
-
-
-
-
preferential release of a C-terminal lysine or arginine amino acid
show the reaction diagram
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
47 kDa zymogen granule membrane associated protein
-
-
-
-
aCAP
-
-
B carboxypeptidase
-
-
carboxypeptidase B
-
-
carboxypeptidase B
-
-
carboxypeptidase B
-
-
carboxypeptidase B
P09955
-
Carboxypeptidase B1
-
-
carboxypeptidase BII
-
-
-
-
CPB
-
-
-
-
CPB
-
-
CPB1
-
-
EC 3.4.12.3
-
-
formerly
-
EC 3.4.2.2
-
-
formerly
-
HBCPB
-
-
Pancreas-specific protein
-
-
-
-
PASP
-
-
-
-
PcpB
-
-
pp-CpB
-
-
protaminase
-
-
-
-
TAFI
-
possesses carboxypeptidase B-like activity
thrombin-activatable fibrinolysis inhibitor
-
-
thrombin-activatable fibrinolysis inhibitor
-
possesses carboxypeptidase B-like activity
thrombin-activatable procarboxypeptidase B
-
-
tissue carboxypeptidase B
-
-
ZAP47
-
-
-
-
additional information
-
the enzyme belongs to the M14A peptidase family
CAS REGISTRY NUMBER
COMMENTARY
9025-24-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
physiological function
-
thrombomodulin suppresses pericellular fibrinolysis and plasma-induced tumor cell invasion, which is mediated by plasma TAFI activation
physiological function
-
thrombin-activatable CPB plays a central homeostatic role in rheumatoid arthritis by regulating neutrophil viability and reducing synoviocyte adhesion
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-(2-furyl)acryloyl-L-Ala-L-Arg + H2O
3-(2-furyl)acryloyl-L-Ala + L-Arg
show the reaction diagram
-
-
-
?
Arg-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
?
show the reaction diagram
-
bradykinin
-
-
?
benzoyl-beta-Ala-L-Lys + H2O
?
show the reaction diagram
-
low activity
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
-
-
-
?
benzoyl-Gly-Gly-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-glycylphenyllactic acid + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-L-Arg + H2O
benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
-
?
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR + H2O
biotin-(epsilon-aminocaproic acid)2-GLMVGGVV + Arg
show the reaction diagram
-
-
-
?
carbobenzoxy-Gly-L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
endostar + H2O
?
show the reaction diagram
-
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
-
-
?
furylacryloylalanylarginine + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloylalanyllysine + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-Gly + H2O
?
show the reaction diagram
-
10% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
-
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
-
mutant enzymes S253K and S253R are inactive
-
-
-
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
Sesamia nonagrioides Lef.
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-arginine + H2O
hippuric acid + L-Arg
show the reaction diagram
P09955
-
-
-
?
hippuryl-L-Asp + H2O
hippuric acid + Asp
show the reaction diagram
-
hydrolyzed by mutant enzyme D253K and mutant enzyme D253R, wild type enzyme shows no activity
-
-
?
hippuryl-L-Glu + H2O
hippuric acid + Glu
show the reaction diagram
-
hydrolyzed by mutant enzyme D253K, wild type enzyme shows no activity
-
-
?
hippuryl-L-homoarginine + H2O
hippuric acid + homoarginine
show the reaction diagram
-
low activity
-
-
?
hippuryl-L-Orn + H2O
hippuric acid + Orn
show the reaction diagram
-
-
-
-
?
hippuryl-L-Phe + H2O
?
show the reaction diagram
-
18% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-L-Pro-L-Lys + H2O
?
show the reaction diagram
-
low activity
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
-
-
-
-
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
-
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
129% of the activity with hippuryl-L-Arg
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
-
peptidase activity
-
-
?
hippurylphenyllactic acid + H2O
hippuric acid + phenyllactic acid
show the reaction diagram
-
-
-
-
?
human insulin-like peptide 3 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
Leu-Asp-Ser + H2O
Leu-Asp + Ser
show the reaction diagram
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
show the reaction diagram
-
-
-
-
?
OPN-R + H2O
OPN-L + ?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
?
mono/di-Arg-insulin + H2O
human insulin
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
the enzyme is specific for COOH-terminal Lys or Arg residues
-
-
-
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 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
?
-
-, Q3T905
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 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
?
-
-, Q3T905
the enzyme is highly specific for excising C-terminal Lys from peptides and protein substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
OPN-R + H2O
OPN-L + ?
show the reaction diagram
-
osteopontin (OPN) gets activated by thrombin resulting in OPN-R. OPN-R is subsequently inactivated by CPB generating OPN-L
-
-
?
human proinsulin + H2O
?
show the reaction diagram
-
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
-
-
?
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
?
-
-, Q3T905
the enzyme is involved in digestion processes in the gut supplying free amino acid for developing larvae
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activates
Co2+
-
CoCl2, accelerates hydrolysis of hippuryl-L-Arg and hippuryl-Lys
Co2+
-
1 mM, activation to 181% of control
Co2+
-
activates 1.7fold at 25C and pH 7.5
Zinc
-
contains zinc
Zinc
-
contains 1 gatom of zinc per mol of enzyme
Zinc
-
contains 1 gatom of zinc per mol of enzyme
Zinc
-
0.96 gatom of zinc per mol of enzyme
Zn2+
-
1 mol Zn2+ per mol of enzyme
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
Zn2+
-
zinc-carboxypeptidase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
-
binding structure analysis
(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
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
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-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-Aminohexanoic acid
-
-
6-Aminohexanoic acid
-
-
6-Aminohexanoic acid
-
-
6-guanidinohexanoic acid
-
-
aminobenzylsuccinic acid
-
-
-
antithrombomodulin antibody
-
-
-
Benzamidine
-
-
Beta-phenylpropionic acid
-
-
Ca2+
-
1 mM, 36% inhibition
Co2+
-
hydrolysis of hippuryl-L-Arg
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
binding structure analysis
DL-benzylsuccinic acid
-
-
DL-guanidinoethylmercaptosuccinic acid
-
-
EDTA
-
partial
EDTA
-
1 mM, 6 h, 90% loss of activity
EDTA
-
6 h, 1 mM, 90% inhibition
Epsilon-aminocaproic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
Hg2+
-
1 mM, 90% inhibition
Hg2+
-
1 mM, 97% inhibition
hippuryl-D-Lys
-
-
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
-
-
Phenanthroline
-
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
recombinant protein
-
protamine
-
-
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
P15086
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
-
Mn2+
-
1 mM, 51% inhibition
additional information
-, Q3T905
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
-
the enzyme is down-regulates upon feeding, the enzyme expression in the midgut is affected by ingestion of Plasmodium falciparum
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
allopurinol
-
addition of allopurinol alone and allopurinol plus 5,5-dimethyl-1-pyrroline N-oxide results in increased CPB1 activity
Thrombin
-
-
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
3-(2-furyl)acryloyl-L-Ala-L-Arg
-
-
0.1
-
benzoyl-Gly-Arg
-
soluble enzyme
0.23
-
benzoyl-Gly-Arg
-
soluble enzyme
0.71
-
benzoyl-Gly-Arg
-
-
8
-
benzoyl-Gly-Arg
-
crystallized enzyme
24
-
benzoyl-Gly-Gly-Phe
-
crystallized enzyme
40
-
benzoyl-Gly-Gly-Phe
-
soluble enzyme
3
-
benzoyl-Gly-glycylphenyllactic acid
-
crystallized enzyme
-
80
-
benzoyl-Gly-glycylphenyllactic acid
-
soluble enzyme
-
0.32
-
benzoyl-Gly-L-Arg
-
-
0.008
-
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
-
pH 7.4
80
-
Carbobenzoxy-Gly-Phe
-
soluble enzyme
100
-
Carbobenzoxy-Gly-Phe
-
crystallized enzyme
0.1
-
furylacryloylalanylarginine
-
-
0.12
-
furylacryloylalanylarginine
-
-
0.07
-
furylacryloylalanyllysine
-
-
0.11
-
furylacryloylalanyllysine
-
-
0.277
-
hippuryl-Arg
-
carboxypeptidase B I
0.31
-
hippuryl-Arg
-
carboxypeptidase B II
0.39
-
hippuryl-Arg
-
-
0.54
-
hippuryl-Arg
-
-
0.05
-
hippuryl-L-Arg
-
carboxypeptidase B I
0.053
-
hippuryl-L-Arg
-
-
0.065
-
hippuryl-L-Arg
-
-
0.071
-
hippuryl-L-Arg
-
carboxypeptidase B II
0.08
-
hippuryl-L-Arg
-
-
0.11
-
hippuryl-L-Arg
-
-
0.18
-
hippuryl-L-Arg
-
carboxypeptidase B I
0.18
-
hippuryl-L-Arg
-
-
0.19
-
hippuryl-L-Arg
-
carboxypeptidase B
2.8
-
hippuryl-L-Arg
-
soluble enzyme
28
-
hippuryl-L-Arg
-
immobilized enzyme
2.63
-
hippuryl-Lys
-
-
0.06
-
N-(4-methoxyphenylazoformyl)-Arg
-
-
0.6
-
N-(phenylcarbonyl)glycyl-L-arginine
-
crystallized enzyme
0.15
-
N-benzoylglycyl-L-Arg
-
carboxypeptidase B I and B II
3.55
-
hippuryl-Lys
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km-values of mutant enzymes with hippuryl-Glu as substrate
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.67
-
benzoyl-Gly-Arg
-
crystallized enzyme
60
-
benzoyl-Gly-Arg
-
soluble enzyme
183
-
benzoyl-Gly-Arg
-
soluble enzyme
427
-
benzoyl-Gly-Arg
-
-
0.333
-
benzoyl-Gly-Gly-Phe
-
crystallized enzyme
5.5
-
benzoyl-Gly-Gly-Phe
-
soluble enzyme
2.83
-
benzoyl-Gly-glycylphenyllactic acid
-
crystallized enzyme
-
917
-
benzoyl-Gly-glycylphenyllactic acid
-
soluble enzyme
-
86
-
benzoyl-Gly-L-Arg
-
-
1.9
-
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
-
pH 7.4
2.5
-
carbobenbenzoxy-Gly-Phe
-
crystallized enzyme
104
-
Carbobenzoxy-Gly-Phe
-
soluble enzyme
50
-
furylacryloylalanylarginine
-
-
58.7
-
furylacryloylalanylarginine
-
-
24.6
-
furylacryloylalanyllysine
-
-
38.6
-
furylacryloylalanyllysine
-
-
61
-
hippuryl-Arg
-
-
86.9
-
hippuryl-Arg
-
-
119
-
hippuryl-Arg
-
-
0.16
-
hippuryl-Asp
-
mutant enzyme D253R
0.26
-
hippuryl-Asp
-
mutant enzyme D253K
3.8
-
hippuryl-Glu
-
mutant enzyme D253K
27.4
-
hippuryl-L-Arg
-
-
48.3
-
hippuryl-L-Arg
-
-
171
-
hippuryl-L-Arg
-
-
10.5
-
hippuryl-Lys
-
-
0.667
-
N-(phenylcarbonyl)glycyl-L-arginine
-
crystallized enzyme
53
-
N-benzoylglycyl-L-Arg
-
carboxypeptidase B II
57
-
N-benzoylglycyl-L-Arg
-
carboxypeptidase B I
25.5
-
hippuryl-Lys
-
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2e-06
-
(2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
-
pH 7.4, 22C
0.000206
-
(S)-5-amino-2-((1-propyl-1H-imidazol-4-yl)methyl)pentanoic acid
-
-
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
7e-06
-
2-(2-chloro-5-guanidinophenyl)-3-mercaptopropanoic acid
-
-
3.4e-05
-
2-(2-guanidinoethylthio)succinic acid
-
-
0.004
-
2-(2-guanidinoethylthio)succinic acid
-
-
2e-06
-
2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
-
7e-06
-
2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid
-
pH 7.4, 22C
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
-
-
5e-05
-
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
2e-06
-
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
-
pH 7.4, 22C
4.2e-07
-
5-guanidino-2-(mercaptomethyl)pentanoic acid
-
-
5
-
Benzamidine
-
-
8.2e-06
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
pH 7.4
6.3e-05
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
pH 7.4, 22C
0.01
-
DL-benzylsuccinic acid
-
pH 7.5
0.0119
-
DL-benzylsuccinic acid
-
pH 7.5
0.0011
-
DL-guanidinoethylmercaptosuccinic acid
-
pH 7.5
0.9
-
Epsilon-aminocaproic acid
-
pH 7.4
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
0.275
-
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22C
0.07
-
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22C
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
0.41
-
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
pH 7.5, 22C
0.165
-
methyl N-[[(1R,2S)-2-([N-[(benzyloxy)carbonyl]-beta-alanyl]amino)cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22C
0.4
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22C
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-(3-chlorophenyl)-4-((5-(3-methoxybenzylthio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
-
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
0.043
-
N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22C
0.003
-
N-[[di(propan-2-yl)amino]-[3-(4-methoxyphenyl)-2-trimethylsilyloxiran-2-yl]phosphinothioyl]-N-propan-2-ylpropan-2-amine
-
-
1e-06
-
Potato carboxypeptidase inhibitor
-
pH 7.4
-
1.8e-06
-
Potato carboxypeptidase inhibitor
-
pH 7.4, 23C
-
0.01
-
protamine
-
above, pH 7.4
1.3e-06
-
tick carboxypeptidase inhibitor
-
pH 7.4, 23C
-
0.5
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
pH 7.5, 22C
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
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2e-06
-
(R)-2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
-
0.0023
-
(R)-2-guanidino-3-mercaptopropanoic acid
-
-
2.4e-05
-
2-(4-(furan-2-ylmethyl)-5-(4-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)-1-(thiophen-2-yl)ethanone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25.83
-
-
-
175
-
-
-
862
-
-
carboxypeptidase B I
1192
-
-
carboxypeptidase B II
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
turnover-number of mutant enzymes with hippuryl-Glu
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
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
-
7
-
-
cleavage of hippuryl-L-Arg
7.4
-
-
assay at
7.4
-
-
assay at
7.5
8
-
depending on substrate
7.5
-
-
assay at
7.6
7.7
-
soluble and immobilized enzyme
7.65
-
-
assay at
7.65
-
-
assay at
8.3
-
-
assay at
8.5
-
-
assay at
10
-
-
hydrolysis of hippuryl-L-Arg
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
11
-
high loss of activity below pH 6.0 and above pH 10.0
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
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
assay at
22
-
-
assay at room temperature
23
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
27
-
-
assay at
30
35
-
-
30
-
-
assay at
37
-
-
assay at
48
-
-
soluble enzyme
55
-
-
immobilized enzyme
additional information
-
-
assay at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-
30C: 65% of maximal activity, 60C: 50% of maximal activity
30
70
-
30C: about 40% of maximal activity, 70C: about 55% of maximal activity
30
70
-
inactivation above 50C
35
65
-
35C: 45% of maximal activity, 65C: about 50% of maximal activity, immobilized enzyme
45
80
-
45C: about 35% of maximal activity, 80C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
majority of the enzyme exists in the prepro-form
Manually annotated by BRENDA team
Sesamia nonagrioides Lef.
-
-
-
Manually annotated by BRENDA team
-
longitudinal, of instestine
Manually annotated by BRENDA team
-
pancreatic juice
Manually annotated by BRENDA team
-
carboxypeptidase B from pancreatic tissue, carboxypeptidase B I and B II from pancreatic juice. Carboxypeptidase B is converted to carboxypeptidase B II by trypsin
Manually annotated by BRENDA team
-
the activated carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein
Manually annotated by BRENDA team
-
majority of the enzyme exists in the mature form
Manually annotated by BRENDA team
-
from patients with acute pancreatitis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
fibroblast-like synoviocytes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
-
the enzyme is secreted from pancreas
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27700
-
-
gel filtration
32000
-
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB
32210
-
-
carboxypeptidase B II, gel filtration
32920
-
-
carboxypeptidase B I, gel filtration
34200
-
-
boundary depletion equilibrium sedimentation
34300
-
-
calculation from sedimentation and diffusion data
34300
-
-
calculation from sedimentation and diffusion data
35000
37000
-
equilibrium sedimentation
35000
-
-
SDS-PAGE, activated form
35000
-
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB
47000
-
-
Western Blot analysis, nitrosylated CPB1
57400
-
-
equilibrium sedimentation
58000
-
-
SDS-PAGE
65000
-
-
Western blot analysis
70000
-
-
Western blot analysis, investigation of peroxynitrite-induced chemical nitrosylation of CPB, dimer formation, band immunoreactive to an antibody specific to 3-nitrotyrosine
additional information
-
-
-
additional information
-
-
analysis of active enzyme and inactive proenzyme by gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 32000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
dimer
-
x * 9200 + x * 23500, carboxypeptidase B II, SDS-PAGE
dimer
-
x * 9200 + x * 23500, carboxypeptidase B I, SDS-PAGE after reduction with 2-mercaptoethanol
dimer
-
2 * 35000, SDS-PAGE, dimer formation as a result of dityrosine crosslinks
monomer
-
1 * 31000, SDS-PAGE
monomer
-
1 * 34000, carboxypeptidase B, SDS-PAGE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
the zymogen has a MW of 40000 Da
proteolytic modification
-
40000 Da prepro form of the enzyme, 30000 Da mature enzyme form
proteolytic modification
-
the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin
proteolytic modification
P15086
cleavage and activation of the recombinant zymogen by trypsin
proteolytic modification
-
zymogen activation by trypsin cleaving the activation peptide off the proenzyme at room temperature and pH 8.2
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
proteolytic modification
-
the zymogen has a MW of 45000 Da
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
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 is synthesized as zymogen, cleavage and activation in vitro by trypsin
proteolytic modification
-
the enzyme is produced as secreted pro-enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 20C, X-ray diffraction structure determination and analysis at 2.0 A resolution
P15086
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
30 min, inactivation
5
-
-
the purified enzyme is unstable below
6
10
-
purified enzyme, stable
6
-
-
or above, 6.0 mg/ml protein concentration, stable for several months
6.7
8.8
-
60C, optimal stability of the immobilized enzyme
7.5
-
-
60C, optimal stability of the soluble enzyme
additional information
-
-
pH 4.5 is the optimal pH for immobilization
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
-
stable for at least 1 year, immobilized enzyme
30
45
-
15 min, stable
30
45
-
15 min, purified enzyme, stable
50
-
-
2 h, stable
50
-
-
15 min, little loss of activity
50
-
-
15 min, about 10% loss of activity
50
-
-
15 min, the purified enzyme is unstable above
60
-
-
40 min, more than 50% loss of activity
60
-
-
15 min, 56% loss of activity
60
-
-
15 min, about 70% loss of activity
60
-
-
15 min, loss of 70% of purified enzyme activity
65
-
-
15 min, about 10% loss of activity
70
-
-
15 min, 85% loss of activity
additional information
-
-
heat stability is markedly increased as an effect of immobilization
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
25-45% loss of activity after lyophilization
-
stable to several thawings and refreezings
-
at low protein concentration, 0.05 mg/ml, stable for at least 1 month
-
freezing and thawing has no effect
-
heat stability is markedly increased as an effect of immobilization
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for 2-4 weeks
-
frozen or precipitated purified pancreatic enzyme is stable for years
-
frozen, stable for up to 1 year
-
20-25C, stable for at least 1 year, immobilized enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity chromatography
-
affinity chromatography; large-scale; multiple forms: carboxypeptidase B I and B II
-
native enzyme from pancreatic acetine powder
-
from gut by affinity chromatography
-, Q3T905
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
-
native enzyme 418fold from pyloric ceca to near homogeneity by gel filtration, anion exchange chromatography, and another step of gel filtration
-
procarboxypeptidase B
-
further purification of the commercial pancreatic preparation by hydrophobic interaction chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA sequence determination, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, expression of the zymogen in Pichia pastoris
-, Q3T905
DNA sequence determination, phylogenetic tree
-
recombinant expression of the zymogen in Pichia pastoris straim KM71
P15086
recombinantly expressed
-
DNA sequence determination, phylogenetic tree
-
DNA and amino acid sequence determination and analysis of midgut carboxypeptidase B
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
the enzyme is a serum marker for acute pancreatitis and pancreatic graft injection
drug development
P15086
the enzyme is a target for design of active site inhibitors based on the structure of tick carboxypeptidase inhibitor, a potential antithrombolytic drug
analysis
-
the immobilized carboxypeptidase B is used for stepwise digestion of cytochrome c
synthesis
-
production of human insulin