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Information on EC 3.4.17.3 - lysine carboxypeptidase and Organism(s) Mus musculus and UniProt Accession Q9JJN5

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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
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This record set is specific for:
Mus musculus
UNIPROT: Q9JJN5 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Release of a C-terminal basic amino acid, preferentially lysine
Synonyms
carboxypeptidase n, kininase i, procpb, anaphylatoxin inactivator, carboxypeptidase n1, bradykininase, cpase n, creatine kinase conversion factor, lysine carboxypeptidase, kininase ia, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxypeptidase N
-
anaphylatoxin inactivator
-
-
-
-
Arginine carboxypeptidase
-
-
-
-
bradykinase
-
-
-
-
bradykinin-decomposing enzyme
-
-
-
-
bradykininase
-
-
-
-
carboxypeptidase B
-
-
carboxypeptidase N
carboxypeptidase, arginine
-
-
-
-
CPase N
-
-
-
-
CPN1
-
-
creatine kinase conversion factor
-
-
-
-
creatinine kinase convertase
-
-
-
-
hippuryllysine hydrolase
-
-
-
-
kininase I
-
-
-
-
kininase Ia
-
-
-
-
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
plasma carboxypeptidase
-
-
Plasma carboxypeptidase B
-
-
-
-
protaminase
-
-
-
-
SCPN
-
-
-
-
thrombin-activatable carboxypeptidase B
-
-
thrombin-activatable fibrinolysis inhibitor
-
-
thrombin-activatable procarboxypeptidase B
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9013-89-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-
-
?
activated complement C3a + H2O
?
show the reaction diagram
-
-
-
-
?
activated complement C5a + H2O
?
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
His-tagged C3f peptide + H2O
?
show the reaction diagram
-
CPN cleaves the C-terminal Arg of C3f_R1310-R1320 to produce C3f_R1310-L1319
-
-
?
thrombin-cleaved osteopontin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
zinc-metalloprotease
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DL-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
potato carboxypeptidase inhibitor
-
-
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thrombin-thrombomodulin complex
-
on the vascular endothelial surface
-
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
weak expression
Manually annotated by BRENDA team
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
fetal
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
constitutive expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
additional information
the enzyme is constitutively active
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPN_MOUSE
457
0
51845
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
2 * 52000, the homodimeric enzyme consists of two small subunits
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 52000, the homodimeric enzyme consists of two small subunits
additional information
-
subunit interaction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
gene structure comparison, DNA and amino acid sequence determination and analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
data support the thesis that thrombin-activable CPB has broad anti-inflammatory properties
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
785-793
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team