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 (Engineering
Engineering on EC 3.4.17.22 - metallocarboxypeptidase D
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R166A/R169A
enzyme is cleaved by furin. Proteins sequence reveals a consensus sequence for furin cleavage (RXXR) at positions 166 to 169. Cleavage at this site removes the N-terminal 169 residues to generate a truncated protein of approximately 151 kDa. Substitution of the two arginines with alanine completely abolishes cleavage of DCPD
E350Q
E350Q/E762Q
E762Q
additional information
E350Q
critical active site residue in domain I, displays more than 50% activity from pH 5.0-7.5, similar to wild-type
E350Q
pH optimum of mutant enzyme is identical to wild-type enzyme, pH-range with 50% of maximal activity is pH 5.0-7.5 compared to pH 5.0-7.0 for wild-type enzyme
E350Q/E762Q
completely inactive towards all substrates and at all pH values tested
E350Q/E762Q
no detectable enzyme activity at any of the pH values examined
E762Q
critical active site residue in domain II, displays more than 50% activity from pH 6.5 to 7.5
E762Q
pH optimum of mutant enzyme is pH 7.0, compared to pH 6.5 for wild-type enzyme. pH-range with 50% of maximal activity is pH 6.5-7.5 compared to pH 5.0-7.0 for wild-type enzyme
additional information
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duck CPD (dCPD) like all other CPDs identified, consists of three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each, one transmembrane domain and a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network. While two of the three luminal/extracellular domains bind Zn2+-ions and exhibit enzymatic carboxypeptidase activity towards yet unidentified cellular proteins that cross the secretory pathway, the membrane proximal C-domain of dCPD is enzymatically inactive and binds duck hepatitis B virus-preS polypeptide with very high affinity
additional information
duck CPD (dCPD) like all other CPDs identified, consists of three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each, one transmembrane domain and a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network. While two of the three luminal/extracellular domains bind Zn2+-ions and exhibit enzymatic carboxypeptidase activity towards yet unidentified cellular proteins that cross the secretory pathway, the membrane proximal C-domain of dCPD is enzymatically inactive and binds duck hepatitis B virus-preS polypeptide with very high affinity
additional information
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a noninfectious pre-S deletion mutant devoid of the binding region for carboxypeptidase D can be rendered infectious for primary duck hepatocytes by treatment with chymotrypsin
additional information
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CPD mutant lacking the cytoplasmic trans-Golgi network-retrieval signal into primary duck hepatocytes, abolishes duck hepatitis B virus infection of transduced cells
additional information
CPD mutant lacking the cytoplasmic trans-Golgi network-retrieval signal into primary duck hepatocytes, abolishes duck hepatitis B virus infection of transduced cells
additional information
svrPG33 mutants, do not survive past the early larval stage. These mutants have a P-element insertion within exon 1B upstream of the initiation ATG, which greatly reduces mRNA levels of all forms of CPD. Both svr1 and svrpoi mutants are viable, both deletions eliminate enzyme activity of the second CP-like domain and appear to cause the misfolding of the protein. This greatly reduces the levels of the long forms of CPD protein but do not affect the levels of the short forms
additional information
enzyme with mutations in both domains I and II is completely inactive towards all substrates and at all pH values
additional information
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enzyme with mutations in both domains I and II is completely inactive towards all substrates and at all pH values
