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Information on EC 3.4.17.3 - lysine carboxypeptidase
for references in articles please use BRENDA:EC3.4.17.3
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.17 Metallocarboxypeptidases
3.4.17.3 lysine carboxypeptidase
IUBMB Comments
A zinc enzyme found in plasma. Inactivates bradykinin and anaphylatoxins in blood plasma. In peptidase family M14 (carboxypeptidase A family).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
showSynonyms
carboxypeptidase n, kininase i, procpb, anaphylatoxin inactivator, carboxypeptidase n1, bradykininase, cpase n, creatine kinase conversion factor, lysine carboxypeptidase, kininase ia, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anaphylatoxin inactivator
-
-
-
-
Arginine carboxypeptidase
-
-
-
-
bradykinase
-
-
-
-
bradykinin-decomposing enzyme
-
-
-
-
bradykininase
-
-
-
-
carboxypeptidase B
carboxypeptidase N
carboxypeptidase, arginine
-
-
-
-
CPase N
-
-
-
-
CPB
CPN
CPN1
creatine kinase conversion factor
-
-
-
-
creatinine kinase convertase
-
-
-
-
EC 3.4.12.7
-
-
formerly
-
hippuryllysine hydrolase
-
-
-
-
kininase I
-
-
-
-
kininase Ia
-
-
-
-
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
plasma carboxypeptidase
Plasma carboxypeptidase B
-
-
-
-
protaminase
-
-
-
-
SCPN
-
-
-
-
carboxypeptidase N
-
-
-
-
CPN
-
-
-
-
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Phe-Ser-Pro-Phe-Arg + H2O
acetyl-Phe-Ser-Pro-Phe + Arg
-
Substrates: -
Products: -
Products: -
?
Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
-
Substrates: reaction is less efficient than reaction with EC 3.4.17.20
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Arg + H2O
benzyloxycarbonyl-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
Lys + benzyloxycarbonyl-Val-Gly-Lys
-
Substrates: -
Products: -
Products: -
?
bradykinin + H2O
desArg-bradykinin + L-Arg
-
Substrates: bradykinin is inactivated by proteolysis by the enzyme
Products: -
Products: -
?
dansyl-Phe-Ala-Arg + H2O
dansyl-Phe-Ala + L-arginine
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Gly-Arg + H2O
furylacryloyl-Gly + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Gly-Lys + H2O
furylacryloyl-Gly + Lys
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-L-Ala-L-Lys + H2O
furylacryloyl-L-Ala + Lys
-
Substrates: -
Products: -
Products: -
?
Hippuryl-L-argininic acid + H2O
Hippuric acid + argininic acid
-
Substrates: -
Products: -
Products: -
?
hippuryl-L-His-L-Leu + H2O
hippuryl-L-His + L-Leu
-
Substrates: -
Products: -
Products: -
?
hippuryl-L-Lys-L-Leu + H2O
hippuryl-L-Lys + L-Leu
-
Substrates: -
Products: -
Products: -
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
Substrates: i.e. C5a, reaction is less efficient than reaction with EC 3.4.17.20
Products: -
Products: -
?
His-tagged C3f peptide + H2O
?
-
Substrates: CPN cleaves the C-terminal Arg of C3f_R1310-R1320 to produce C3f_R1310-L1319
Products: -
Products: -
?
YFPGQFAFSK + H2O
YFPGQFAFS + lysine
Substrates: bioacivity of 10-mer chemerin peptide, chemerin 149-158, is enhanced by removing the carboxyl-terminal lysine
Products: -
Products: -
?
YFPGQFAFSKALPRS + H2O
?
Substrates: sequential cleavage of prochemerin peptide, chemerin 149-163, by CPB increases chemotactic activities
Products: -
Products: -
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
Substrates: -
Products: -
Products: -
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
Substrates: i.e. bradykinin, removal of C-terminal Arg
Products: -
Products: -
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
Substrates: -
Products: -
Products: -
?
C3a69-77 + H2O
?
Substrates: peptide derived from bradykinin
Products: -
Products: -
?
C5a66-74 + H2O
?
Substrates: peptide derived from bradykinin
Products: -
Products: -
?
chemerin + H2O
?
Substrates: CPN enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
Products: -
Products: -
?
chemerin + H2O
?
Substrates: CPB enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
Products: -
Products: -
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
-
Substrates: low reaction rate
Products: -
Products: -
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
Substrates: -
Products: -
Products: -
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
Substrates: -
Products: -
Products: -
?
prochemerin + H2O
?
Substrates: 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
Products: -
Products: -
?
prochemerin + H2O
?
Substrates: sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cleaves C-terminal Lys faster than Arg in most substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme releases C-terminal Arg and Lys from peptide substrates, such as bradykinin, kallidin, or Met-Lys-bradykinin
Products: -
Products: -
?
additional information
?
-
-
Substrates: C-terminal cleavage of stromal cell-derived factor-1alpha reducing the substrate's biological activity, SDF-1alpha
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: carboxypeptidase N is not an acute phase protein under inflammatory conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase N is not an acute phase protein under inflammatory conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme releases C-terminal Arg and Lys from peptide substrates, such as bradykinin, kallidin, or Met-Lys-bradykinin
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: carboxypeptidase N is not an acute phase protein under inflammatory conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase N is not an acute phase protein under inflammatory conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
Products: -
Products: -
?
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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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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Kininase I, kininase II and aminopeptidase levels in patients with gastrointestinal tumors.
Alzheimer Disease
[Activity of peptidyl-dipeptidase A and carboxypeptidase N in the serum of patients with Alzheimer disease]
Anaphylaxis
Plasma protease inhibitor and anaphylatoxin inactivator levels in chronic urticaria/angioedema and in patients experiencing anaphylactoid reactions to radiographic contrast media.
Angina, Unstable
Conversion of MM creatine kinase isoforms in human plasma by carboxypeptidase N.
Angioedema
Examination of baseline levels of carboxypeptidase N and complement components as potential predictors of angioedema associated with the use of an angiotensin-converting enzyme inhibitor.
Arthritis
Carboxypeptidase N (kininase I) activity in blood and synovial fluid from patients with arthritis.
Arthritis, Gouty
Tissue factor pathway inhibitor and thrombin-activatable carboxypeptidase B for prediction of early atherosclerosis in gouty arthritis.
Arthritis, Psoriatic
Carboxypeptidase N (kininase I) activity in blood and synovial fluid from patients with arthritis.
Arthritis, Rheumatoid
Carboxypeptidase N (kininase I) activity in blood and synovial fluid from patients with arthritis.
Arthritis, Rheumatoid
Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis.
Atherosclerosis
Tissue factor pathway inhibitor and thrombin-activatable carboxypeptidase B for prediction of early atherosclerosis in gouty arthritis.
Breast Neoplasms
Circulating proteolytic products of carboxypeptidase N for early detection of breast cancer.
Breast Neoplasms
Serum Carboxypeptidase N 1 Serves as a Potential Biomarker Complementing CA15-3 for Breast Cancer.
Carcinoma, Hepatocellular
A t(3;8) chromosomal translocation associated with hepatitis B virus intergration involves the carboxypeptidase N locus.
Carcinoma, Hepatocellular
Carboxypeptidase H. A regulatory peptide-processing enzyme produced by human hepatoma Hep G2 cells.
Colitis, Ulcerative
Serum angiotensin-I-converting enzyme and carboxypeptidase N in Crohn's disease and ulcerative colitis.
COVID-19
High-dose ACEi might be harmful in COVID-19 patients with serious respiratory distress syndrome by leading to excessive bradykinin receptor activation.
Crohn Disease
Serum angiotensin-I-converting enzyme and carboxypeptidase N in Crohn's disease and ulcerative colitis.
Essential Hypertension
Study on the renal kallikrein-kinin system in normal and low renin subgroups of essential hypertension.
Essential Hypertension
Urinary excretions of kininase I and kininase II activities in essential hypertension. A sensitive and simple method for its kinin-destroying capacity.
Hepatitis
[Value of studying carboxypeptidase N activity in the blood and urine of children with viral hepatitis]
Hepatitis B
A t(3;8) chromosomal translocation associated with hepatitis B virus intergration involves the carboxypeptidase N locus.
Hypersensitivity
Hypersensitivity reactions during haemodialysis: role of complement fragments and ethylene oxide antibodies.
Hypertension
Aldosterone, kallikrein, kininase I and II in normal and hypertension complicated pregnancy.
Hypotension
Effect of DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid on the blood pressure response to vasoactive substances.
Hypotension
Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI).
Infections
High-dose ACEi might be harmful in COVID-19 patients with serious respiratory distress syndrome by leading to excessive bradykinin receptor activation.
lysine carboxypeptidase deficiency
DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency.
lysine carboxypeptidase deficiency
Plasma protease inhibitor and anaphylatoxin inactivator levels in chronic urticaria/angioedema and in patients experiencing anaphylactoid reactions to radiographic contrast media.
Malaria, Cerebral
Deletion of carboxypeptidase N delays onset of experimental cerebral malaria.
Myocardial Infarction
Carboxypeptidase N and creatine kinase-MB isoforms in acute myocardial infarction.
Myocardial Infarction
Characterization of MB creatine kinase isoform conversion in vitro and in vivo in dogs.
Myocardial Infarction
[Changes in the kallikrein-kinin system of the blood during development of experimental myocardial infarct]
Neoplasms
A t(3;8) chromosomal translocation associated with hepatitis B virus intergration involves the carboxypeptidase N locus.
Neoplasms
Kininase I, kininase II and aminopeptidase levels in patients with gastrointestinal tumors.
Nephrotic Syndrome
[State of the kinin system and level of serum proteinase inhibitors in latent nephritis and the nephrotic syndrome of different etiology]
Neutropenia
In vivo effects of C3a on neutrophils and its contribution to inflammatory lung processes in a guinea-pig model.
Osteoarthritis
Carboxypeptidase N (kininase I) activity in blood and synovial fluid from patients with arthritis.
Pancreatitis
[Changes in some of the kallikrein-kinin system indices in patients with acute pancreatitis]
Periodontal Diseases
[Bradykininase activity in gingival fluid in the periodontal disease (author's transl)]
Periodontal Diseases
[Kinin contents and bradykininase activities in whole saliva and ginival fluid from patients with periodontal disease (author's transl)]
Periodontal Diseases
[The variation of bradykininase activity in the pocket exudate of the patients with periodontal disease after scaling and brushing (author's transl)]
Placental Insufficiency
[Proteolytic activity of fetoplacental complex in norm and pathology].
Pre-Eclampsia
Increased serum kininase I activity in pregnancy complicated by pre-eclampsia.
Proteinuria
[State of the kinin system and level of serum proteinase inhibitors in latent nephritis and the nephrotic syndrome of different etiology]
Sepsis
Identification of Potential Biomarkers by Serum Proteomics Analysis in Rats With Sepsis.
Thrombocytopenia
Role of complement-derived peptides in thrombocytopenia elicited by soluble aggregates of immunoglobulin G in the rat.
Thrombosis
Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity.
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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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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
-
-
brenda
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
U3JB00
cpn1 mRNA is expressed in developing vessels of the embryo
brenda
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
brenda
-
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
brenda
-
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
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
among mice genetically deficient in either carboxypeptidase B2 (Cpb2) or carboxypeptidase N (Cpn), in a model of hemolytic-uremic syndrome, Cpb2-/- mice have the worst disease, followed by Cpn-/- mice, with wild-type mice being the most protected. This model is driven by complement component C5a, and shows that carboxypeptidase B2 is important in inactivating complement component C5a. Cpn-/- mice are generated by disruption of complement component Cpn1. When mice are challenged acutely with cobra venom factor, the reverse phenotype is observed. Cpn-/- mice have markedly worse disease than Cpb2-/- mice, and wild-type mice are resistant
malfunction
U3JB00
the knockdown of cpn1 by morpholino injection impairs the growth of intersegmental vessels and caudal vein plexus. Loss of cpn1 affects the expression of the vascular markers flt4, mrc1, flk, stabilin, and ephrinb2
malfunction
-
enzyme deficiency causes an increase in vascular leakage from failure to convert bradykinin to desArg-bradykinin
physiological function
the enzyme removes C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them
physiological function
carboxypeptidase N is responsible for systemic inactivation of complement component C3a and C5a
physiological function
U3JB00
cpn1 is involved in vascular development of zebrafish
physiological function
-
the enzyme regulates biologically active peptides, including complement anaphylatoxins and kinins, by removing carboxy-terminal arginine or lysine. The enzyme is a very important part of the body's defense against the build-up of potentially harmful peptides that normally act as autocrine or paracrine hormones in the area
Show AA Sequence and Transmembrane Helices (507 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
315000
45000
48000
50000
52000
83000
90000
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 * 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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
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
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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
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
-
the enzyme activity is significantly reduced gender-independently in COVID-19 and returns to normal during convalescence
-
there is a significant increase in enzyme level post-vitamin D supplementation. The enzyme is significantly inversely correlated to nitric oxide in males after vitamin D supplementation
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
data support the thesis that thrombin-activable CPB has broad anti-inflammatory properties
medicine
-
serum enzyme activity correlates with disease severity in COVID-19 patients
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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
brenda
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
-
brenda
Plummer, T.H.; Erdös, E.G.
Human plasma carboxypeptidase N
Methods Enzymol.
80
442-449
1981
Homo sapiens
brenda
Plummer, T.H.; Hurwitz, M.Y.
Human plasma carboxypeptidase N. Isolation and characterization
J. Biol. Chem.
253
3907-3912
1978
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
Oshima, G.; Kato, J.; Erdös, E.G.
Plasma carboxypeptidase N, subunits and characteristics
Arch. Biochem. Biophys.
170
132-138
1975
Homo sapiens
brenda
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
-
brenda
Hendriks, D.; Scharpe, S.; van Sande, M.
Carboxypeptidase N activity in human tissues and fluids
Biochem. Soc. Trans.
14
1048
1986
Homo sapiens
-
brenda
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
brenda
Jeanneret, L.; Roth, M.; Bargetzi, J.P.
Carboxypeptidase N from pig serum
Hoppe-Seyler's Z. Physiol. Chem.
357
867-872
1976
Sus scrofa
brenda
Juillerat-Jeanneret, L.; Roth, M.; Bargetzi, J.P.
Some properties of porcine carboxypeptidase N
Hoppe-Seyler's Z. Physiol. Chem.
363
51-58
1982
Sus scrofa
brenda
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
brenda
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
brenda
Plummer, T.H.; Kimmel, M.T.
An improved spectrophotometric assay for human plasma carboxypeptidase N1
Anal. Biochem.
108
348-353
1980
Homo sapiens
brenda
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
brenda
Koheil, A.; Forstner, G.
Isoelectric focusing of carboxypeptidase N
Biochim. Biophys. Acta
524
156-161
1978
Homo sapiens
brenda
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
brenda
Linder, L.E.; Sund, M.L.; Lönnies, H.
Isolation and purification of cell wall-associated arginine carboxypeptidase from Streptococcus mitis ATCC 15909
Curr. Microbiol.
28
91-96
1994
Streptococcus mitis
-
brenda
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
brenda
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
brenda
Barabe, J.; Huberdeau, D.
A micromethod for the determination of the activities of kininases in rat plasma. Kinetics and inhibitory characteristics
Biochem. Pharmacol.
41
821-827
1991
Rattus norvegicus
brenda
Orawski, A.T.; Susz, J.P.; Simmons, W.H.
Metabolism of bradykinin by multiple coexisting membrane-bound peptidases in lung: techniques for investigating the role of each peptidase using specific inhibitors
Adv. Exp. Med. Biol.
247B
355-364
1989
Rattus norvegicus, Bos taurus
brenda
Schweisfurth, H.
Carboxypeptidase N
Dtsch. Med. Wochenschr.
109
1254-1258
1984
Homo sapiens
brenda
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
brenda
Sato, T.; Miwa, T.; Akatsu, H.; Matsukawa, N.; Obata, K.; Okada, N.; Campbell, W.; Okada, H.
Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not
J. Immunol.
165
1053-1058
2000
Mus musculus (Q9JJN5), Mus musculus
brenda
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
brenda
Kato, T.; Akatsu, H.; Sato, T.; Matsuo, S.; Yamamoto, T.; Campbell, W.; Hotta, N.; Okada, N.; Okada, H.
Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N
Microbiol. Immunol.
44
719-728
2000
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
Matthews, K.W.; Drouin, S.M.; Liu, C.; Martin, J.F.; Skidgel, R.A.; Wetsel, R.A.
Expression of the third complement component (C3) and carboxypeptidase N small subunit (CPN1) during mouse embryonic development
Dev. Comp. Immunol.
28
647-655
2004
Mus musculus
brenda
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
785-793
2004
Mus musculus, Homo sapiens
brenda
Leung, L.L.; Nishimura, T.; Myles, T.
Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI)
Adv. Exp. Med. Biol.
632
61-69
2008
Mus musculus
brenda
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)
brenda
Leung, L.L.; Myles, T.; Nishimura, T.; Song, J.J.; Robinson, W.H.
Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI)
Mol. Immunol.
45
4080-4083
2008
Mus musculus
brenda
Talens, S.; Lebbink, J.H.; Malfliet, J.J.; Demmers, J.A.; Uitte de Willige, S.; Leebeek, F.W.; Rijken, D.C.
Binding of carboxypeptidase N to fibrinogen and fibrin
Biochem. Biophys. Res. Commun.
427
421-425
2012
Homo sapiens
brenda
Li, Y.; Li, Y.; Chen, T.; Kuklina, A.S.; Bernard, P.; Esteva, F.J.; Shen, H.; Ferrari, M.; Hu, Y.
Circulating proteolytic products of carboxypeptidase N for early detection of breast cancer
Clin. Chem.
60
233-242
2014
Mus musculus
brenda
Helwig, M.; Herwig, A.; Heldmaier, G.; Barrett, P.; Mercer, J.G.; Klingenspor, M.
Photoperiod-dependent regulation of carboxypeptidase E affects the selective processing of neuropeptides in the seasonal Siberian hamster (Phodopus sungorus)
J. Neuroendocrinol.
25
190-197
2013
Phodopus sungorus
brenda
Leung, L.L.K.; Morser, J.
Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity
J. Thromb. Haemost.
16
1474-1486
2018
Mus musculus (Q9JJN5)
brenda
Wu, T.Y.; Wang, Y.S.; Song, Y.C.; Chen, Z.Y.; Chen, Y.T.; Chiu, C.C.; Wu, C.Y.
Fine-tune regulation of carboxypeptidase N1 controls vascular patterning during zebrafish development
Sci. Rep.
7
1852
2017
Danio rerio (U3JB00), Danio rerio
brenda
Yakout, S.M.; Abdi, S.; Alaskar, A.H.; Khattak, M.N.K.; Al-Masri, A.A.; Al-Daghri, N.M.
Impact of vitamin D status correction on serum lipid profile, carboxypeptidase N and nitric oxide levels in Saudi adults
Int. J. Mol. Sci.
24
7711
2023
Homo sapiens
brenda
Tepasse, P.R.; Vollenberg, R.; Steinebrey, N.; Koenig, S.
High angiotensin-converting enzyme and low carboxypeptidase N serum activity correlate with disease severity in COVID-19 patients
J. Pers. Med.
12
406
2022
Homo sapiens
brenda
Zhou, Q.; Zhao, L.; Shao, Z.; Declerck, P.; Leung, L.L.K.; Morser, J.
Both plasma basic carboxypeptidases, carboxypeptidase B2 and carboxypeptidase N, regulate vascular leakage activity in mice
J. Thromb. Haemost.
20
238-244
2022
Mus musculus
brenda
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