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Information on EC 3.4.17.3 - lysine carboxypeptidase and Organism(s) Rattus norvegicus

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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:
Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
anaphylatoxin inactivator
-
-
-
-
Arginine carboxypeptidase
-
-
-
-
bradykinase
-
-
-
-
bradykinin-decomposing enzyme
-
-
-
-
bradykininase
-
-
-
-
carboxypeptidase N
carboxypeptidase, arginine
-
-
-
-
CPase N
-
-
-
-
creatine kinase conversion factor
-
-
-
-
creatinine kinase convertase
-
-
-
-
hippuryllysine hydrolase
-
-
-
-
kininase I
-
-
-
-
kininase Ia
-
-
-
-
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
Plasma carboxypeptidase B
-
-
-
-
protaminase
-
-
-
-
SCPN
-
-
-
-
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
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuryl-L-His + L-Leu
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
show the reaction diagram
-
-
-
-
?
hippuryl-L-Lys-L-Leu + H2O
hippuryl-L-Lys + L-Leu
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.0128 mM
phosphormaidon
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.93
hippuryl-L-Arg
-
-
35.8
Hippuryl-L-Lys
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPN_RAT
457
0
51981
Swiss-Prot
Secretory Pathway (Reliability: 1)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
no loss of activity for up to 25 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in CHO cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barabe, J.; Huberdeau, D.
A micromethod for the determination of the activities of kininases in rat plasma. Kinetics and inhibitory characteristics
Biochem. Pharmacol.
41
821-827
1991
Rattus norvegicus
Manually annotated by BRENDA team
Orawski, A.T.; Susz, J.P.; Simmons, W.H.
Metabolism of bradykinin by multiple coexisting membrane-bound peptidases in lung: techniques for investigating the role of each peptidase using specific inhibitors
Adv. Exp. Med. Biol.
247B
355-364
1989
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
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
J. Pharmacol. Exp. Ther.
309
607-615
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
Microbiol. Immunol.
44
719-728
2000
Rattus norvegicus
Manually annotated by BRENDA team
Komura, H.; Shimomura, Y.; Yumoto, M.; Katsuya, H.; Okada, N.; Okada, H.
Heat stability of carboxypeptidase R of experimental animals
Microbiol. Immunol.
46
217-223
2002
Cavia porcellus, Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team