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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-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
-
-
-
-
?
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-Ala-Arg + H2O

benzoyl-Ala + Arg
-
-
-
-
-
benzoyl-Ala-Arg + H2O
benzoyl-Ala + Arg
-
-
-
-
?
benzoyl-Ala-Lys + H2O

?
-
-
-
-
-
benzoyl-Ala-Lys + H2O
?
-
-
-
-
?
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-Arg + H2O

furylacryloyl-Ala + Arg
-
-
-
-
-
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O

furylacryloylalanine-Ala + Lys
-
-
-
-
-
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-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.
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.
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.
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.
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).
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
Plasma carboxypeptidases as regulators of the plasminogen system.
Urticaria
Familial carboxypeptidase N deficiency.
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
brenda
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