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acetyl-Phe-Ser-Pro-Phe-Arg + H2O
acetyl-Phe-Ser-Pro-Phe + Arg
-
-
-
-
?
activated complement C3a + H2O
?
-
-
-
-
?
activated complement C5a + H2O
?
-
-
-
-
?
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
-
?
anaphylatoxin + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
benzoyl-Ala-Arg + H2O
benzoyl-Ala + Arg
-
-
-
-
?
benzoyl-Ala-Lys + H2O
?
-
-
-
-
?
benzoyl-argininic acid + H2O
?
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
benzyloxycarbonyl-Ala-Arg + H2O
benzyloxycarbonyl-Ala + Arg
-
-
-
-
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
Lys + benzyloxycarbonyl-Val-Gly-Lys
-
-
-
?
dansyl-Phe-Ala-Arg + H2O
dansyl-Phe-Ala + L-arginine
-
-
-
-
?
fibrinopeptide A + H2O
Arg + ?
-
very low activity
-
?
fibrinopeptide alphaArg96-104 + H2O
?
-
-
-
?
fibrinopeptide B + H2O
Arg + ?
-
-
-
?
fibrinopeptide betaLys125-133 + H2O
?
-
-
-
?
fibrinopeptide gammaLys54-62 + H2O
?
-
-
-
?
fibrinopeptide gammaLys77-85 + H2O
?
-
-
-
?
fibrinopeptide-alpha-Arg96-104 + H2O
?
-
-
-
?
fibrinopeptide-beta-Lys125-133 + H2O
?
-
-
-
?
fibrinopeptide-gamma-Lys54-62 + H2O
?
-
-
-
?
fibrinopeptide-gamma-Lys77-85 + H2O
?
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
furylacryloyl-Gly-Arg + H2O
furylacryloyl-Gly + Arg
-
-
-
-
?
furylacryloyl-Gly-Lys + H2O
furylacryloyl-Gly + Lys
-
-
-
-
?
furylacryloyl-L-Ala-L-Lys + H2O
furylacryloyl-L-Ala + Lys
-
-
-
-
?
Gly-His-Lys + H2O
Gly-His + Lys
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
Hippuryl-L-argininic acid + H2O
Hippuric acid + argininic acid
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuryl-L-His + L-Leu
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
hippuryl-L-Lys-L-Leu + H2O
hippuryl-L-Lys + L-Leu
-
-
-
-
?
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
-
-
?
kallikrein + H2O
?
-
plasma or urinary
-
-
?
Leu-Trp-Met-Arg + H2O
Leu-Trp-Met + Arg
-
-
-
?
Phe-Ser-Pro-Phe-Arg + H2O
Phe-Ser-Pro-Phe + Arg
-
-
-
-
?
plasmin + H2O
?
-
-
-
-
?
Pro-Gly-Lys-Ala-Arg + H2O
Pro-Gly-Lys-Ala + Arg
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro-Phe-Gly + Lys
-
-
-
?
Pro-Phe-Lys + H2O
Pro-Phe + Lys
-
-
-
-
?
Pro-Phe-Lys-Gly + H2O
Pro-Phe-Lys + Gly
-
-
-
-
?
salmine + H2O
Arg + ?
-
-
-
?
Thr-Pro-Arg-Lys + H2O
Thr-Pro-Arg + Lys
-
-
-
?
thrombin-cleaved osteopontin + H2O
?
-
-
-
-
?
trypsin + H2O
?
-
-
-
-
?
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
-
-
?
additional information
?
-
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
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
-
-
-
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
-
-
-
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
inactivates bradykinin
-
-
?
bradykinin + H2O
?
-
-
-
-
?
C3a69-77 + H2O
?
-
-
-
?
C3a69-77 + H2O
?
peptide derived from bradykinin
-
-
?
C5a66-74 + H2O
?
-
-
-
?
C5a66-74 + H2O
?
peptide derived from bradykinin
-
-
?
chemerin + H2O
?
-
-
-
?
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
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
-
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
-
low reaction rate
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
-
?
polylysine + H2O
Lys
-
-
-
-
?
polylysine + H2O
Lys
-
-
-
?
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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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
Aggregate anaphylaxis and carboxypeptidase N.
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.
Angioedema
Familial carboxypeptidase N deficiency.
Angioedema
The role of complement in urticaria and angioedema.
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
Role of carboxypeptidase N invasion and migration in 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.
Chronic Urticaria
Familial carboxypeptidase N deficiency.
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.
Cushing Syndrome
Significance of renal kininases in patients with Cushing's syndrome.
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.
Fetal Hypoxia
Umbilical plasma kininase I activity in fetal hypoxia.
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.
Hyperaldosteronism
Significance of renal kininases in patients with primary aldosteronism.
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.
Hypertension
Lead-induced hypertension: role of oxidative stress.
Hypertension
Pathogenesis of lead-induced hypertension: role of oxidative stress.
Hypertension
Significance of renal kininases in patients with Cushing's syndrome.
Hypertension
Significance of renal kininases in patients with primary aldosteronism.
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.
Lung Diseases
Kininase I and II activities in serum of patients with lung diseases.
lysine carboxypeptidase deficiency
DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency.
lysine carboxypeptidase deficiency
Familial carboxypeptidase N deficiency.
lysine carboxypeptidase deficiency
Major 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.
Neoplasms
Role of carboxypeptidase N invasion and migration in breast cancer.
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.
Pre-Eclampsia
Umbilical plasma kininase I activity in fetal hypoxia.
Proteinuria
[State of the kinin system and level of serum proteinase inhibitors in latent nephritis and the nephrotic syndrome of different etiology]
Sarcoidosis
[Changes in serum carboxypeptidase N in patients with lung sarcoidosis]
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.
Thrombosis
Plasma carboxypeptidases as regulators of the plasminogen system.
Urticaria
The role of complement in urticaria and angioedema.
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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
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