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Information on EC 3.4.17.22 - metallocarboxypeptidase D and Organism(s) Rattus norvegicus and UniProt Accession Q9JHW1

for references in articles please use BRENDA:EC3.4.17.22
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.22 metallocarboxypeptidase D
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q9JHW1 not found.
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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releases C-terminal Arg and Lys from polypeptides
Synonyms
silver, gp180, cpd-n, metallocarboxypeptidase d, carboxypeptidase-d, duck carboxypeptidase d, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxypeptidase-D
-
Carboxypeptidase D
-
-
-
-
carboxypeptidase-D
-
-
CPD
-
-
-
-
gp180
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
153967-26-1
not distinguished from EC 3.4.16.6 in Chemical Abstracts
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
show the reaction diagram
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
1,10-phenanthroline
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.063
Dansyl-Ala-Arg
0.1 M sodium acetate, 37°C
0.132
Dansyl-Ala-Arg
0.1 M sodium acetate, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0451
1,10-phenanthroline
-
0.0476
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
0.0116
1,10-phenanthroline
-
0.0093
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
domain I is most active at pH 7 whereas domain II is most active at pH 5.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
also detectable in the cytosol after 24 h treatment with interleukin-2
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPD_RAT
1378
1
152616
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
SDS-PAGE
160000
SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Song, L.; Fricker, L.D.
Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D
J. Biol. Chem.
271
28884-28889
1996
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Xin, X.; Varlamov, O.; Day, R.; Bridgett, M.M.; Leiter, E.H.; Fricker, L.D.
Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D
DNA Cell Biol.
16
897-909
1997
Rattus norvegicus
Manually annotated by BRENDA team
O'Malley, P.G.; Sangster, S.M.; Abdelmagid, S.A.; Bearne, S.L.; Too, C.K.
Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells
Biochem. J.
390
665-673
2005
Rattus norvegicus, Rattus norvegicus (Q9JHW1)
Manually annotated by BRENDA team