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Information on EC 3.4.17.3 - lysine carboxypeptidase
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EC Tree
3.4.17.3 lysine carboxypeptidaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
carboxypeptidase n, kininase i, procpb, anaphylatoxin inactivator, carboxypeptidase n1, bradykininase, cpase n, creatine kinase conversion factor, lysine carboxypeptidase, kininase ia, 
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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
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
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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
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-
-
-
?
chemerin + H2O
?
CPB enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
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-
?
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
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-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
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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
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-
?
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
?
-
-
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
?
-
-
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]
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 carboxype