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Information on EC 3.4.17.22 - metallocarboxypeptidase D and Organism(s) Homo sapiens and UniProt Accession O75976

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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:
Homo sapiens
UNIPROT: O75976 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
-
-
gp180
-
-
-
-
metallocarboxypeptidase-D
-
-
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-Phe-Ala-Arg + H2O
Dansyl-Phe-Ala + Arg
show the reaction diagram
-
-
-
?
Dansyl-Phe-Gly-Arg + H2O
Dansyl-Phe-Gly + Arg
show the reaction diagram
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
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
?
-
-
releases C-terminal arginine or lysine from polypeptides
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
MGTA
siRNA
downregulation of CpD by siRNA leads to downregulation of transforming growth factor-beta
-
small interfering CPD RNA
-
siCPD RNA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-estradiol
-
up-regulates CPD mRNA and protein expression
prolactin
-
up-regulates CPD mRNA and protein expression
-
transforming growth factor-beta
leads to upregulation of CpD in primary human blood monocytes. Does not upregulate CpD in HepG2 cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.153 - 0.844
dansyl-Phe-Ala-Arg
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7 - 12.5
dansyl-Phe-Ala-Arg
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8 - 82
dansyl-Phe-Ala-Arg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
mutant enzyme E762Q
6.4
-
placenta
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
enzyme with all three domains intact and enzyme with mutation of domain I display more than 50% activity from pH 5.0 to 7.5
5 - 7.5
6.5 - 7.5
mutant enzyme E762Q displays more than 50% activity from pH 6.5 to 7.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
it is demonstrated that CpD is up-regulated by TGF-beta in CD14 + human blood monocytes
Manually annotated by BRENDA team
baseline expression
Manually annotated by BRENDA team
-
overexpressed in hepatocellular carcinoma
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
metallocarboxypeptidase D is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways
Manually annotated by BRENDA team
metallocarboxypeptidase D is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways
Manually annotated by BRENDA team
-
trans-Golgi network
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
together with the differences in pH optima, the different substrate specificities of CPD domains I and II allow the enzyme to perform distinct functions in the various locations within the cell
malfunction
-
knockdown of endogenous CPD expression in Huh7 HCC cells by RNA interference reduces cell proliferation, blocks the cell cycle at G1 phase, and increases apoptosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPD_HUMAN
1380
1
152931
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175000
-
x * 175000, SDS-PAGE
180000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparative modeling of the active sites of CPD domains I, II and III and molecular docking of peptide substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E350Q
E350Q/E762Q
E762Q
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
human carboxypeptidase D (residues 32-1298) is cloned into the pTriExTM-7 expression vector that encodes an IgM secretion signal sequence and an N-terminal Strep-Tag II fusion protein. The CPD-pTrieX-7 construct ias transfected into mammalian HEK293F cells for transient expression, using polyethylenimine as transfection reagent
transfection of HEK-293F cell
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpressed in hepatocellular carcinoma
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tan, F.; Rehli, M.; Krause, S.W.; Skidgel, R.A.
Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains
Biochem. J.
327
81-87
1997
Homo sapiens
Manually annotated by BRENDA team
McGwire, G.B.; Tan, F.; Michael, B.; Rehli, M.; Skidgel, R.A.
Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein
Life Sci.
60
715-724
1997
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Yamashita, M.; Sano, T.; Qian, Z.R.; Kovacs, K.; Horvath, E.
Diversity of ACTH- immunoreactive cells in the human adenohypophysis: an immunohistochemical study with special reference to cluster formation and follicular cell association
Endocr. Pathol.
17
155-164
2006
Homo sapiens
Manually annotated by BRENDA team
Hoff, N.P.; Degrandi, D.; Hengge, U.; Pfeffer, K.; Wurthner, J.U.
Carboxypeptidase D: a novel TGF-beta target gene dysregulated in patients with lupus erythematosus
J. Clin. Immunol.
27
568-579
2007
Homo sapiens, Homo sapiens (O75976), Mus musculus
Manually annotated by BRENDA team
Glebe, D.; Urban, S.
Viral and cellular determinants involved in hepadnaviral entry
World J. Gastroenterol.
13
22-38
2007
Anas platyrhynchos, Anas platyrhynchos (Q90240), Gallus gallus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Abdelmagid, S.A.; Too, C.K.
Prolactin and estrogen up-regulate carboxypeptidase-D to promote nitric oxide production and survival of MCF-7 breast cancer cells
Endocrinology
149
4821-4828
2008
Homo sapiens
Manually annotated by BRENDA team
Jin, T.; Fu, J.; Feng, X.J.; Wang, S.M.; Huang, X.; Zhu, M.H.; Zhang, S.H.
SiRNA-targeted carboxypeptidase D inhibits hepatocellular carcinoma growth
Cell Biol. Int.
37
929-939
2013
Homo sapiens
Manually annotated by BRENDA team
Thomas, L.N.; Chedrawe, E.R.; Barnes, P.J.; Too, C.K.L.
Prolactin/androgen-inducible carboxypeptidase-D increases with nitrotyrosine and Ki67 for breast cancer progression in vivo, and upregulates progression markers VEGF-C and Runx2 in vitro
Breast Cancer Res. Treat.
164
27-40
2017
Homo sapiens (O75976), Homo sapiens
Manually annotated by BRENDA team
Garcia-Pardo, J.; Tanco, S.; Diaz, L.; Dasgupta, S.; Fernandez-Recio, J.; Lorenzo, J.; Aviles, F.X.; Fricker, L.D.
Substrate specificity of human metallocarboxypeptidase D Comparison of the two active carboxypeptidase domains
PLoS ONE
12
e0187778
2017
Homo sapiens (O75976), Homo sapiens
Manually annotated by BRENDA team
Thomas, L.N.; Merrimen, J.; Bell, D.G.; Rendon, R.; Too, C.K.
Prolactin- and testosterone-induced carboxypeptidase-D correlates with increased nitrotyrosines and Ki67 in prostate cancer
Prostate
75
1726-1736
2015
Homo sapiens (O75976)
Manually annotated by BRENDA team