3.4.17.22: metallocarboxypeptidase D
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3.4.17.22
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- 3.4.17.22
- nanoparticles
-
agnps
- gold
- nitrate
-
film
-
fabric
-
plasmonic
-
electrode
-
raman
-
colloid
- staphylococcus
- aureus
- copper
- devices
-
uv-vis
-
impregnation
-
nanostructures
-
dress
-
nanocomposite
-
electrochemical
- fiber
-
nanomaterials
-
glass
-
fourier
- grain
-
infrared
-
spherical
-
bactericidal
- burn
-
autoradiograph
-
wavelength
-
graphene
- mercury
-
nanoscale
- teeth
-
transparent
-
silicon
-
print
-
biocompatibility
-
nucleolar
-
porous
-
immerse
-
titanium
-
biomedical
-
self-assembled
- medicine
-
nanotube
-
nanocrystals
-
disinfect
-
tunable
- dentin
Reaction
releases C-terminal Arg and Lys from polypeptides =
Synonyms
Carboxypeptidase D, carboxypeptidase-D, CPD, CPD-N, DCPD, duck carboxypeptidase D, gp180, metallocarboxypeptidase-D, More, p170, silver, svr
ECTree
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
medicine
additional information
Drosophila CPD is encoded by the silver gene svr, which is differentially spliced to produce long transmembrane protein forms with three metallocarboxypeptidase-like domains and short soluble forms with a single metallocarboxypeptidase domain. Flies that retain the short form are viable, whereas flies that are missing all forms of CPD do not survive past the early larval stages
medicine
CpD is significantly downregulated in CD14 positive cells isolated from patients with lupus erythematosus. Moreover, it is shown that downregulation of CpD leads to downmodulation of TGF-beta itself, suggesting a role for CpD in a positive feedback loop, providing further evidence for a role of this enzyme in lupus erythematosus
medicine
for duck hepatitis B virus and probably all other avian hepadnaviruses, carboxypeptidase D (CPD) is shown to be indispensable for infection. The striking correlation of the infection competition activity of duck hepatitis B virus-preS polypeptides with their ability to bind duck carboxypeptidase D suggests that it is this molecule which is addressed and inactivated at the surface of hepatocytes
medicine
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CpD is part of an autoregulatory feedback loop in which it is both upstream and downstream of transforming growth factor-beta signaling
medicine
CpD is part of the transforming growth factor-beta pathway and is dysregulated in patients with Lupus erythematosus and other autoimmune diseases
medicine
CPE, probably in combination with CPD, has a functional role in normal placental development, specifically in control of giant cell and glycogen cell growth. In addition, Cpe together with Cpd is an upstream determinant of interspecies hybrid placental dysplasia, whose lack produces placental phenotypes reminiscent of interspecies hybrid placental dysplasia. Pathways regulated by these enzymes are not only important in placentation, but potentially also for speciation in the genus Mus
medicine
essential for duck hepatitis B virus infection. PreS-induced CPD conformational changes may play an important role in the fusion of the viral and cellular membrane
medicine
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for infection of primary duck hepatocytes with duck hepatitis B virus, binding of the pre-S domain of the large surface protein to the cellular glycoprotein gp180 as a ubiquitous carboxypeptidase is required
medicine
CPD, nitrotyrosine, and proliferation marker Ki67 levels are higher in prostate cancer than in benign tissue and tend to colocalize, along with phospho-Stat5. The CPD-Arg-NO pathway may be involved in the regulation of prostate cancer cell proliferation
medicine
knocking out CpD gene expression provides one solution to eliminating C-terminal lysine heterogeneity for therapeutic antibody production
medicine
The CPD-Arg-nitric oxide pathway contributes to breast cancer progression in vitro and in vivo. There are progressive increases in CPD, nitrotyrosine, Ki67, and Cullin-3 from low levels in benign tissues to high levels in ductal carcinoma in situ, low-grade, high-grade, and triple-negative breast cancer. CPD and nitrotyrosine staining are closely associated, implicating CPD in nitric oxide production
