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 hide
3.4.17.2
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase B
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential release of a C-terminal lysine or arginine amino acid
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-24-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cpbAg1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
low levels of carboxypeptidase B
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
starfish
-
-
Manually annotated by BRENDA team
rumen bacterium
-
-
-
Manually annotated by BRENDA team
Salaria basilisca
-
-
-
Manually annotated by BRENDA team
Lef.
-
-
Manually annotated by BRENDA team
Lef.
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA
-
-
?
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 + H2O
Hippuric acid + L-Arg
show the reaction diagram
hippuryl-L-arginine + H2O
hippuric acid + L-Arg
show the reaction diagram
-
-
-
?
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-Lys
hippuric acid + L-Lys
show the reaction diagram
-
-
-
?
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
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
-
-
-
?
mono/di-Arg-insulin + H2O
human insulin
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
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
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrin + H2O
?
show the reaction diagram
-
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
(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-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
2-(2-chloro-5-guanidinophenyl)-3-mercaptopropanoic acid
-
-
2-(2-guanidinoethylthio)succinic acid
-
-
2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
-
2-(4-(furan-2-ylmethyl)-5-(4-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)-1-(thiophen-2-yl)ethanone
-
-
2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid
-
binding structure analysis
2-(6,9-dimethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)-1-(4-fluorophenyl)ethanone
-
-
2-benzyl-3-mercaptopropanoic acid
-
-
2-Guanidinoethylmercaptosuccinic acid
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
2-mercaptomethyl-5-guanidinopentanoic acid
3-(6-amino-5-chloropyridin-3-yl)-2-(selanylmethyl)propanoic acid
-
-
3-Phenylpropanoic acid
-
-
3-Phenylpropionic acid
-
-
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
-
5-aminopentanoic acid
-
-
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
-
binding structure analysis
5-guanidino-2-(mercaptomethyl)pentanoic acid
-
-
6-Amino-n-hexanoic acid
-
-
6-Aminohexanoic acid
6-guanidinohexanoic acid
-
-
7-amino-2-(selanylmethyl)heptanoic acid
-
-
7-amino-2-(sulfanylmethyl)heptanoic acid
-
-
7-amino-2-[(propanoylselanyl)methyl]heptanoic acid
-
-
aminobenzylsuccinic acid
-
-
-
antithrombomodulin antibody
-
-
-
benzamidine
-
-
Beta-phenylpropionic acid
-
-
Ca2+
-
1 mM, 36% inhibition
Co2+
-
hydrolysis of hippuryl-L-Arg
Cu2+
Salaria basilisca
-
inhibits activity
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
DL-benzylsuccinic acid
DL-guanidinoethylmercaptosuccinic acid
-
-
Epsilon-aminocaproic acid
-
-
Guanidinoethylmercaptosuccinic acid
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
protamine
-
-
tick carboxypeptidase inhibitor
Urea
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
allopurinol
-
addition of allopurinol alone and allopurinol plus 5,5-dimethyl-1-pyrroline N-oxide results in increased CPB1 activity
L-Cys
-
activates
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
3-(2-furyl)acryloyl-L-Ala-L-Arg
-
-
0.1 - 8
benzoyl-Gly-Arg
24 - 40
benzoyl-Gly-Gly-Phe
3 - 80
benzoyl-Gly-glycylphenyllactic acid
0.32
benzoyl-Gly-L-Arg
-
-
0.008
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
-
pH 7.4
80 - 100
Carbobenzoxy-Gly-Phe
0.1 - 0.12
furylacryloylalanylarginine
0.07 - 0.11
furylacryloylalanyllysine
0.277 - 0.54
hippuryl-Arg
0.05 - 28
hippuryl-L-Arg
2.63 - 3.55
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
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.67 - 427
benzoyl-Gly-Arg
0.333 - 5.5
benzoyl-Gly-Gly-Phe
2.83 - 917
benzoyl-Gly-glycylphenyllactic acid
86
benzoyl-Gly-L-Arg
Protopterus aethiopicus
-
-
1.9
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
Homo sapiens
-
pH 7.4
2.5
carbobenbenzoxy-Gly-Phe
Bos taurus
-
crystallized enzyme
104
Carbobenzoxy-Gly-Phe
Bos taurus
-
soluble enzyme
50 - 58.7
furylacryloylalanylarginine
24.6 - 38.6
furylacryloylalanyllysine
61 - 119
hippuryl-Arg
0.16 - 0.26
hippuryl-Asp
3.8
hippuryl-Glu
Homo sapiens
-
mutant enzyme D253K
27.4 - 171
hippuryl-L-Arg
10.5 - 25.5
hippuryl-Lys
0.667
N-(phenylcarbonyl)glycyl-L-arginine
Bos taurus
-
crystallized enzyme
53 - 57
N-benzoylglycyl-L-Arg
additional information
additional information
Scyliorhinus canicula
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5488
hippuryl-L-Arg
Anopheles stephensi
F1ALX3
pH 8, 37C
2744
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000002
(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 - 0.0075
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
0.000007
2-(2-chloro-5-guanidinophenyl)-3-mercaptopropanoic acid
-
-
0.000034 - 0.004
2-(2-guanidinoethylthio)succinic acid
0.000002
2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
-
0.000007
2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid
-
pH 7.4, 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
-
-
0.00005
2-Guanidinoethylmercaptosuccinic acid
-
pH 7.4
0.0014
4-(5-(2-chlorobenzylthio)-1,3,4-oxadiazol-2-yl)-N-(thiophen-2-ylmethyl)benzensulfonamide
-
pH 7.5
0.000002
5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid
-
pH 7.4, 22C
0.00000042
5-guanidino-2-(mercaptomethyl)pentanoic acid
-
-
5
benzamidine
-
-
0.0000082 - 0.000063
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
0.01 - 0.0119
DL-benzylsuccinic acid
0.0011
DL-guanidinoethylmercaptosuccinic acid
-
pH 7.5
0.9
Epsilon-aminocaproic acid
-
pH 7.4
0.0074 - 0.0361
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
0.275
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22C
0.07
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22C
0.0049 - 0.0416
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
0.41
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
pH 7.5, 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
0.5
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
pH 7.5, 22C
0.0012 - 0.0036
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
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
-
-
0.000001 - 0.0000018
Potato carboxypeptidase inhibitor
0.01
protamine
-
above, pH 7.4
0.0000013
tick carboxypeptidase inhibitor
-
pH 7.4, 23C
-
additional information
additional information
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.000002
(R)-2-(3-guanidinophenyl)-3-mercaptopropanoic acid
Sus scrofa
-
-
0.0023
(R)-2-guanidino-3-mercaptopropanoic acid
Sus scrofa
-
-
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
0.0000011
7-amino-2-[(propanoylselanyl)methyl]heptanoic acid
Sus scrofa
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175
-
-
862
-
carboxypeptidase B I
1192
-
carboxypeptidase B II
2757
substrate: hippuryl-L-Lys, pH 8, 37C
15200
substrate: hippuryl-L-Arg, pH 8, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
7
-
cleavage of hippuryl-L-Arg
7.5 - 7.8
-
assay at
7.5
-
assay at
7.5 - 7.8
-
assay at
7.5 - 7.8
-
assay at
7.5 - 8
-
depending on substrate
7.5 - 7.8
-
assay at
7.5 - 8
-
depending on substrate
7.6 - 7.7
-
soluble and immobilized enzyme
8 - 8.5
-
-
8.3
-
assay at
8.5
-
assay at
10
-
hydrolysis of hippuryl-L-Arg
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
assay at
22
-
assay at room temperature
23
-
assay at
27
-
assay at
30
-
assay at
30 - 35
-
-
48
-
soluble enzyme
60
Salaria basilisca
-
-
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
30 - 60
-
30C: 65% of maximal activity, 60C: 50% of maximal activity
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
COMMENTARY hide
LITERATURE
SOURCE
-
majority of the enzyme exists in the prepro-form
Manually annotated by BRENDA team
-
longitudinal, of instestine
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
fibroblast-like synoviocytes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
34500
Salaria basilisca
-
SDS-PAGE
35000 - 37000
-
equilibrium sedimentation
47000
-
Western Blot analysis, nitrosylated CPB1
48100
calculated from cDNA
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrosylation
proteolytic modification
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 20C, 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
-
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
30 min, inactivation
668692
6
-
or above, 6.0 mg/ml protein concentration, stable for several months
36330
6 - 10
-
purified enzyme, stable
668692
6.7 - 8.8
-
60C, optimal stability of the immobilized enzyme
36380
7.5
-
60C, optimal stability of the soluble enzyme
36380
additional information
-
pH 4.5 is the optimal pH for immobilization
36380
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 25
-
stable for at least 1 year, immobilized enzyme
30 - 45
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
LITERATURE
25-45% loss of activity after lyophilization
-
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
-
stable to several thawings and refreezings
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20-25C, stable for at least 1 year, immobilized enzyme
-
4C, stable for 2-4 weeks
-
frozen or precipitated purified pancreatic enzyme is stable for years
-
frozen, stable for up to 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
affinity chromatography; large-scale; multiple forms: carboxypeptidase B I and B II
-
from gut by affinity chromatography
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 enzyme from pancreatic acetine powder
-
native proenzyme from pancreatic juice, separation of active enzyme and inactive proenzyme by gel filtration
-
procarboxypeptidase B
-
purified by chromatography on Q-Sepharose Fast Flow, Heparin-Sepharose CL-6B, Sephacryl S-300, and plasminogen-Sepharose columns
-
using affinity chromatography and gel filtration
-
using ammonium sulfate precipitation and gel filtration
Salaria basilisca
-
using Ni-NTA chromatography
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
expressed in Escherichia coli as a His-tagged fusion protein
recombinant expression of the zymogen in Pichia pastoris straim KM71
recombinantly expressed
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
LITERATURE
analysis
-
the immobilized carboxypeptidase B is used for stepwise digestion of cytochrome c
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
synthesis
-
production of human insulin