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Information on EC 3.4.17.3 - lysine carboxypeptidase and Organism(s) Homo sapiens and UniProt Accession P15169
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3.4.17.3 lysine carboxypeptidaseSpecify your search results
Word Map
- 3.4.17.3
- angiotensin
- anaphylatoxins
- endopeptidase
-
angiotensin-converting
- captopril
- c3a
- kallikrein
-
fibrinolysis
- phosphoramidon
-
kallikrein-kinin
-
procarboxypeptidase
- mergetpa
- angioedema
-
dl-2-mercaptomethyl-3-guanidinoethylthiopropanoic
- hippuryl-l-arginine
-
des-arg9-bk
-
bradykinin-induced
- enkephalinase
- enalaprilat
- prekallikrein
- des-arg9-bradykinin
-
3.4.15.1
- kallidin
- amastatin
- tafia
- kininogenase
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
carboxypeptidase n, kininase i, procpb, anaphylatoxin inactivator, carboxypeptidase n1, bradykininase, cpase n, creatine kinase conversion factor, lysine carboxypeptidase, kininase ia, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anaphylatoxin inactivator
-
-
-
-
Arginine carboxypeptidase
-
-
-
-
bradykinase
-
-
-
-
bradykinin-decomposing enzyme
-
-
-
-
bradykininase
-
-
-
-
carboxypeptidase N
carboxypeptidase, arginine
-
-
-
-
CPase N
-
-
-
-
CPN
creatine kinase conversion factor
-
-
-
-
creatinine kinase convertase
-
-
-
-
hippuryllysine hydrolase
-
-
-
-
kininase I
-
-
-
-
kininase Ia
-
-
-
-
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
Plasma carboxypeptidase B
-
-
-
-
protaminase
-
-
-
-
SCPN
-
-
-
-
carboxypeptidase N
-
-
-
-
CPN
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9013-89-2
-
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
chemerin + H2O
?
CPN enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
-
-
?
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
-
-
?
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
-
?
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
-
?
prochemerin + H2O
?
sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities
-
-
?
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
-
-
?
chemerin + H2O
?
CPB 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
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zinc
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DL-2-mercaptomethyl-3 guanidinoethylthiopropanoic acid
specific inhibitor for CPN but not CPB
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00593 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CBPN_HUMAN
458
0
52286
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
48000
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
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
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
carbohydrate accounts for 17% of the weight, contains significant amounts
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
-
sialoprotein with at least two forms, differing in sialic acid content. Sialic acid may possibly influence stability
side-chain modification
-
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
-
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable in blood plasma for up to seven days after blood collection
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from serum 175.5fold by ammonium sulfate fractionation, anion exchange chromatography and lysine affinity chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene structure comparison, DNA and amino acid sequence determination and analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryan, J.
Arginine carboxypeptidase and its inhibitors
Methods Enzymol.
163
186-194
1988
Homo sapiens
Skidgel, R.A.; Erdös, E.G.
Carboxypeptidase N (arginine carboxypeptidase)
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
60-72
1984
Homo sapiens
-
Plummer, T.H.; Erdös, E.G.
Human plasma carboxypeptidase N
Methods Enzymol.
80
442-449
1981
Homo sapiens
Plummer, T.H.; Hurwitz, M.Y.
Human plasma carboxypeptidase N. Isolation and characterization
J. Biol. Chem.
253
3907-3912
1978
Homo sapiens
Fricker, L.D.; Plummer, T.H.; Snyder, S.H.
Enkephalin convertase: potent, selective, and irreversible inhibitors
Biochem. Biophys. Res. Commun.
111
994-1000
1983
Homo sapiens
Tan, F.; Weerasinghe, D.K.; Skidgel, R.A.; Tamei, H.; Kaul, R.K.; Roninson, I.B.; Schilling, J.W.; Erdös, E.G.
The deduced protein sequence of the human carboxypeptidase N high molecular weight subunit reveals the presence of leucine-rich tandem repeats [published erratum appears in J Biol Chem 1990 Jul 25;265(21):12749
J. Biol. Chem.
265
13-19
1990
Homo sapiens
Levin, Y.; Skidgel, R.A.; Erdös, E.G.
Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i)
Proc. Natl. Acad. Sci. USA
79
4618-4622
1982
Homo sapiens
Oshima, G.; Kato, J.; Erdös, E.G.
Plasma carboxypeptidase N, subunits and characteristics
Arch. Biochem. Biophys.
170
132-138
1975
Homo sapiens
Oshima, G.; Kato, J.; Erdös, E.G.
Subunits of human plasma carboxypeptidase N (kininase I, anaphylatoxin inactivator)
Biochim. Biophys. Acta
365
344-348
1974
Homo sapiens, Sus scrofa
-
Hendriks, D.; Scharpe, S.; van Sande, M.
Carboxypeptidase N activity in human tissues and fluids
Biochem. Soc. Trans.
14
1048
1986
Homo sapiens
-
Grimwood, B.G.; Plummer, T.H.; Tarentino, A.L.
Characterization of the carboxypeptidase N secreted by Hep G2 cells
J. Biol. Chem.
263
14397-14401
1988
Homo sapiens
Moriguchi, M.; Umeda, Y.; Miyazaki, K.; Nakamura, T.; Ogawa, K.; Kojima, F.; Iinuma, H.; Aoyagi, T.
Synthesis of histargin and related compounds and their inhibition of enzymes
J. Antibiot.
41
1823-1827
1988
Homo sapiens
Gebhard, W.; Schube, M.; Eulitz, M.
cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)
Eur. J. Biochem.
178
603-607
1989
Homo sapiens
Plummer, T.H.; Kimmel, M.T.
An improved spectrophotometric assay for human plasma carboxypeptidase N1
Anal. Biochem.
108
348-353
1980
Homo sapiens
Hendriks, D.; Scharpe, S.; van Sande, M.
Assay of carboxypeptidase N activity in serum by liquid-chromatographic determination of hippuric acid
Clin. Chem.
31
1936-1939
1985
Homo sapiens
Koheil, A.; Forstner, G.
Isoelectric focusing of carboxypeptidase N
Biochim. Biophys. Acta
524
156-161
1978
Homo sapiens
Skidgel, R.A.; Weerasinghe, D.K.; Erdös, E.G.
Structure of human carboxypeptidase N (kininase I)
Adv. Exp. Med. Biol.
247A
325-329
1989
Homo sapiens
Wang, W.; Hendriks, D.F.; Scharpe, S.L.
Immobilized carboxypeptidase N. A potent bioreactor and specific adsorbent for peptides
Appl. Biochem. Biotechnol.
44
151-160
1994
Homo sapiens
McCleave, M.J.; Elliott, R.J.; Archbold, G.P.
Human plasma carboxypeptidase N; stability of enzyme activity following collection
Biochem. Soc. Trans.
24
42S
1996
Homo sapiens
Schweisfurth, H.
Carboxypeptidase N
Dtsch. Med. Wochenschr.
109
1254-1258
1984
Homo sapiens
Lazoura, E.; Campbell, W.; Yamaguchi, Y.; Kato, K.; Okada, N.; Okada, H.
Rational structure-based design of a novel carboxypeptidase R inhibitor
Chem. Biol.
9
1129-1139
2002
Homo sapiens
Suzuki, K.; Muto, Y.; Fushihara, K.; Kanemoto, K.; Iida, H.; Sato, E.; Kikuchi, C.; Matsushima, T.; Kato, E.; Nomoto, M.; Yoshioka, S.; Ishii, H.
Enhancement of fibrinolysis by EF6265 [(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxypho sphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B
J. Pharmacol. Exp. Ther.
309
607-615
2004
Homo sapiens, Rattus norvegicus
Campbell, W.D.; Lazoura, E.; Okada, N.; Okada, H.
Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
Microbiol. Immunol.
46
131-134
2002
Homo sapiens
Komura, H.; Shimomura, Y.; Yumoto, M.; Katsuya, H.; Okada, N.; Okada, H.
Heat stability of carboxypeptidase R of experimental animals
Microbiol. Immunol.
46
217-223
2002
Cavia porcellus, Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
Davis, D.A.; Singer, K.E.; De La Luz Sierra, M.; Narazaki, M.; Yang, F.; Fales, H.M.; Yarchoan, R.; Tosato, G.
Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
Blood
105
4561-4568
2005
Homo sapiens
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
785-793
2004
Homo sapiens, Mus musculus
Du, X.Y.; Zabel, B.A.; Myles, T.; Allen, S.J.; Handel, T.M.; Lee, P.P.; Butcher, E.C.; Leung, L.L.
Regulation of chemerin bioactivity by plasma carboxypeptidase N, carboxypeptidase B (activated thrombin-activable fibrinolysis inhibitor), and platelets
J. Biol. Chem.
284
751-758
2009
Homo sapiens, Homo sapiens (P15169)
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