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Enzyme Nomenclature
Information on EC 3.4.17.3 - lysine carboxypeptidase
for references in articles please use BRENDA:EC3.4.17.3
Word Map on EC 3.4.17.3
- 3.4.17.3
- angiotensin
-
anaphylatoxins
-
endopeptidase
-
angiotensin-converting
- captopril
-
kallikrein
-
fibrinolysis
- phosphoramidon
-
kallikrein-kinin
- mergetpa
-
procarboxypeptidase
-
dl-2-mercaptomethyl-3-guanidinoethylthiopropanoic
- hippuryl-l-arginine
-
bradykinin-induced
-
des-arg9-bk
- enalaprilat
-
3.4.15.1
- des-arg9-bradykinin
- enkephalinase
-
prekallikrein
- kallidin
- angioedema
- tafia
- amastatin
- kininogenase
- medicine
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.4.17.3
-
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RECOMMENDED NAME
GeneOntology No.
lysine carboxypeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of a C-terminal basic amino acid, preferentially lysine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9013-89-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
36393, 36394, 36395, 36396, 36397, 36398, 36399, 36400, 36401, 36402, 36403, 36406, 36407, 36408, 36410, 36411, 36412, 36414, 36415, 36418, 650827, 653008, 653144, 653145, 668070, 670291, 698988, 731248
-
-
the enzyme exists in two forms: carboxypeptidase N1, and carboxypeptidase N2 which can be differentiated by their activities towards hippuryl-L-Arg and hippuryl-L-Lys
-
-
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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
Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
-
reaction is less efficient than reaction with EC 3.4.17.20
-
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
Lys + benzyloxycarbonyl-Val-Gly-Lys
-
-
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, reaction is less efficient than reaction with EC 3.4.17.20
-
?
His-tagged C3f peptide + H2O
?
-
CPN cleaves the C-terminal Arg of C3f_R1310-R1320 to produce C3f_R1310-L1319
-
-
?
YFPGQFAFSK + H2O
YFPGQFAFS + lysine
bioacivity of 10-mer chemerin peptide, chemerin 149-158, is enhanced by removing the carboxyl-terminal lysine
-
-
?
YFPGQFAFSKALPRS + H2O
?
sequential cleavage of prochemerin peptide, chemerin 149-163, by CPB increases chemotactic activities
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. bradykinin, removal of C-terminal Arg
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
-
-
-
?
chemerin + H2O
?
CPB enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
-
-
?
chemerin + H2O
?
CPN enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
-
low reaction rate
-
?
prochemerin + H2O
?
sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities
-
-
?
prochemerin + H2O
?
sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities. Endogenous CPN present in circulating plasma enhances the activity of plasmin-cleaved prochemerin
-
-
?
additional information
?
-
-
the enzyme cleaves C-terminal Lys faster than Arg in most substrates
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
-
-
-
additional information
?
-
-
C-terminal cleavage of stromal cell-derived factor-1alpha reducing the substrate's biological activity, SDF-1alpha
-
-
-
additional information
?
-
-
the enzyme releases C-terminal Arg and Lys from peptide substrates, such as bradykinin, kallidin, or Met-Lys-bradykinin
-
-
-
additional information
?
-
-
CPN is identified as a fibrin clot-bound protein using Western blotting. Using surface plasmon resonance it is shown CPN can bind to fibrinogen as well as to fibrin
-
-
-
additional information
?
-
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
the enzyme releases C-terminal Arg and Lys from peptide substrates, such as bradykinin, kallidin, or Met-Lys-bradykinin
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
-
-
-
additional information
?
-
-
CPN is identified as a fibrin clot-bound protein using Western blotting. Using surface plasmon resonance it is shown CPN can bind to fibrinogen as well as to fibrin
-
-
-
additional information
?
-
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
-
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zinc
Zn2+
additional information
-
metalloenzyme, methyl is tightly bound to the apoenzyme at neutral pH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Argininic acid
-
inhibition of peptidase activity and esterase activity; with benzoyl-Gly-Lys, hippuryl-argininic acid or with benzoyl-Gly-Arg as substrate
DL-2-mercaptomethyl-3 guanidinoethylthiopropanoic acid
specific inhibitor for CPN but not CPB
6-aminohexanoic acid
-
with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00593 mM
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.0128 mM
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00593
EF6265
Homo sapiens
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00593 mM
0.0128
EF6265
Rattus norvegicus
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.0128 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison of serum and plasma enzyme activities using substrate stromal cell-derived factor-1alpha
additional information
-
higher activity is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
pH 5.5: about 65% of maximal activity, pH 8.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
-
developmental expression of the enzyme small subunit CPN1, CPN1 expression proceeds the expression of the third complement component C3 by several days, RNA in situ hybridization
-
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
-
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
48000
50000
52000
83000
90000
150000 - 160000
-
ultracentrifugal analysis, a second molecular weight species of 300000-320000 Da is detected
300000 - 320000
-
ultracentrifugal analysis, a second molecular weight species of 150000-160000 Da is detected
315000
48000
-
2 * 48000 + 2 * 83000, the 48000 Da subunit is as active as the intact enzyme, the 83000 Da subunit is inactive but stabilizes the 48000 Da subunit, SDS-PAGE
50000
-
2 * 83000 + 2 * 50000, the two high molecular weight subunits, 58762 Da determined by calculation from nucleotide sequence, protect the two 50000 Da subunits, and keep them into circulation
83000
-
2 * 83000 + 2 * 50000, the two high molecular weight subunits, 58762 Da determined by calculation from nucleotide sequence, protect the two 50000 Da subunits, and keep them into circulation
83000
-
2 * 48000 + 2 * 83000, the 48000 Da subunit is as active as the intact enzyme, the 83000 Da subunit is inactive but stabilizes the 48000 Da subunit, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
tetramer
-
2 * 83000 + 2 * 50000, the two high molecular weight subunits, 58762 Da determined by calculation from nucleotide sequence, protect the two 50000 Da subunits, and keep them into circulation
tetramer
-
2 * 48000 + 2 * 83000, the 48000 Da subunit is as active as the intact enzyme, the 83000 Da subunit is inactive but stabilizes the 48000 Da subunit, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
presence of significant amounts of glucosamine, mannose, galactose, fucose, sialic acid; the carbohydrate is primarily attached to the larger subunit, representing 28% of its weight. Two forms detected in isoelectric focusing with pI of 3.8 and 4.3. The difference is attributed to differences in sialic acid content of the two forms
side-chain modification
-
carbohydrate accounts for 17% of the weight, contains significant amounts; presence of significant amounts of glucosamine, mannose, galactose, fucose, sialic acid
side-chain modification
-
the enzyme contains seven potential N-linked glycosylation sites and a threonine/serine-rich region which is a potential site for attachment of O-linked carbohydrate
side-chain modification
-
sialoprotein with at least two forms, differing in sialic acid content. Sialic acid may possibly influence stability
side-chain modification
-
the 83000 Da subunit contains about 27% carbohydrate per weight, it may contain both N-linked and O-linked carbohydrate
side-chain modification
-
the 90000 Da subunit contains carbohydrate, no carbohydrate is detected in the subunits of MW 50000 Da and 30000 Da
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
room temperature, pH 4-5, 1 h, the 48000 Da subunit loses 94% of its activity, the intact enzyme loses 9% of its activity
37
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable in blood plasma for up to seven days after blood collection
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from serum 175.5fold by ammonium sulfate fractionation, anion exchange chromatography and lysine affinity chromatography to homogeneity
-
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene structure comparison, DNA and amino acid sequence determination and analysis
gene structure comparison, DNA and amino acid sequence determination and analysis
-
gene structure comparison, DNA and amino acid sequence determination and analysis
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
data support the thesis that thrombin-activable CPB has broad anti-inflammatory properties
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.17.3)
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