3.4.17.22: metallocarboxypeptidase D
This is an abbreviated version!
For detailed information about metallocarboxypeptidase D, go to the full flat file.
Word Map on EC 3.4.17.22
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3.4.17.22
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nanoparticles
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agnps
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gold
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nitrate
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film
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fabric
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plasmonic
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electrode
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raman
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colloid
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staphylococcus
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aureus
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copper
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devices
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uv-vis
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impregnation
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nanostructures
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dress
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nanocomposite
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electrochemical
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fiber
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nanomaterials
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glass
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fourier
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grain
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infrared
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spherical
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bactericidal
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burn
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autoradiograph
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wavelength
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graphene
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mercury
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nanoscale
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teeth
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transparent
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silicon
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print
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biocompatibility
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nucleolar
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porous
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immerse
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titanium
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biomedical
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self-assembled
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medicine
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nanotube
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nanocrystals
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disinfect
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tunable
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dentin
- 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
3.4.17.22 metallocarboxypeptidase DAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.17.22 - metallocarboxypeptidase D
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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
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + H2O
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly + Lys
adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD
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?
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys-Arg + H2O
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + Arg
adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD
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additional information
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enzyme is involved in targeting duck hepatitis B virus particles to the secretary pathway for proteolytic cleavage of the viral envelope protein
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additional information
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two of the three luminal/extracellular domains exhibit enzymatic carboxypeptidase activity towards unidentified cellular proteins that cross the secretory pathway. The membrane proximal C-domain of CPD is enzymatically inactive and binds duck hepatitis B virus preS with very high affinity
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?
additional information
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two of the three luminal/extracellular domains exhibit enzymatic carboxypeptidase activity towards unidentified cellular proteins that cross the secretory pathway. The membrane proximal C-domain of CPD is enzymatically inactive and binds duck hepatitis B virus preS with very high affinity
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?
additional information
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the enzyme removes only the C-terminal Lys or Arg from peptides, with the first domain more efficient towards Arg and the second domain more efficient towards Lys. Peptides containing Pro in the penultimate position are poorly cleaved. Cleavage of a peptide with Ala in the penultimate position is most efficient, with the order of decreasing efficiency Ala, Met, Ser, Phe, tyr, Trp, Thr, Gln, Asp, Leu, Gly, Pro. There are only minor differences between the first and the second domains regarding the influence of the penultimate amino acid
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?
additional information
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the enzyme plays a role in processing of many proteins that transit the secretory pathway
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?
additional information
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production of growth factors and/or growth factor receptors, processing of peptide hormones
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?
additional information
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displays only a very weak binding with duck hepatitis B virus preS
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?
additional information
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does not interact with duck hepatitis B virus preS
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additional information
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releases C-terminal arginine or lysine from polypeptides
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additional information
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CPD cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II
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?
additional information
?
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CPD cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II
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?
additional information
?
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multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. The enzyme cleaves exclusively C-terminal basic residues. A quantitative peptidomics approach is used to compare the activities of CPD domains I and II towards a large number of peptides. the enzyme cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II, showing the importance of the P1 position for CPD activity. The preference of domain I for C-terminal Arg is validated through molecular docking experiments
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?
additional information
?
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multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. The enzyme cleaves exclusively C-terminal basic residues. A quantitative peptidomics approach is used to compare the activities of CPD domains I and II towards a large number of peptides. the enzyme cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II, showing the importance of the P1 position for CPD activity. The preference of domain I for C-terminal Arg is validated through molecular docking experiments
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?
additional information
?
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does not interact with duck hepatitis B virus preS
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?
