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Information on EC 3.4.17.3 - lysine carboxypeptidase
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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
-
kallikrein
-
fibrinolysis
- phosphoramidon
-
kallikrein-kinin
- mergetpa
-
procarboxypeptidase
-
des-arg9-bk
-
bradykinin-induced
- hippuryl-l-arginine
-
dl-2-mercaptomethyl-3-guanidinoethylthiopropanoic
- des-arg9-bradykinin
- kallidin
- amastatin
- angioedema
-
3.4.15.1
-
prekallikrein
- enalaprilat
- enkephalinase
- tafia
- kininogenase
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
carboxypeptidase n, kininase i, procpb, anaphylatoxin inactivator, bradykininase, cpase n, creatine kinase conversion factor, kininase ia, thrombin-activatable carboxypeptidase b, 
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
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
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 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
-
-
-
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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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]
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.
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.
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.
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).
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, 731248
-
-
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
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
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
-
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A0H3CAM5_CAUVN
Caulobacter vibrioides (strain NA1000 / CB15N)
432
0
45390
TrEMBL
D5E0T1_BACMQ
Bacillus megaterium (strain ATCC 12872 / QMB1551)
337
0
37721
TrEMBL
C8T679_KLEPR
235
0
25628
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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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SUBUNIT
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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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
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Homo sapiens
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Lazoura, E.; Campbell, W.; Yamaguchi, Y.; Kato, K.; Okada, N.; Okada, H.
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Homo sapiens
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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
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Mus musculus, Mus musculus (Q9JJN5)
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
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Homo sapiens, Rattus norvegicus
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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
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44
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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
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2002
Homo sapiens
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Komura, H.; Shimomura, Y.; Yumoto, M.; Katsuya, H.; Okada, N.; Okada, H.
Heat stability of carboxypeptidase R of experimental animals
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46
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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
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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
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2004
Mus musculus
brenda
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
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2004
Homo sapiens, Mus musculus
brenda
Leung, L.L.; Nishimura, T.; Myles, T.
Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI)
Adv. Exp. Med. Biol.
632
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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
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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
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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
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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
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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
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