Information on EC 3.4.16.6 - carboxypeptidase D

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.4.16.6
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase D
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential release of a C-terminal arginine or lysine residue
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
153967-26-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
cytokine-inducible isoform CPD-N with incomplete N-terminal domain and intact domains II and III
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-factor-Lys-Arg + H2O
mature active alpha-factor + Lys + Arg
show the reaction diagram
-
maturation takes place in sequential manner
-
?
angiotensin 1 + H2O
?
show the reaction diagram
-
truncated KexA releases amino acid residues from the C terminus of angiotensin I
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + L-arginine
show the reaction diagram
-
enzyme shows very low activity
-
-
?
benzoyl-Phe-Ala-Arg + H2O
benzoyl-Phe-Ala + Arg
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Lys + H2O
benzyloxycarbonyl-Gly + L-lysine
show the reaction diagram
-
enzyme shows very low activity
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + L-leucine
show the reaction diagram
-
enzyme shows very low activity
-
-
?
benzyloxycarbonyl-Phe-Tyr-Leu + H2O
benzyloxycarbonyl-Phe-Tyr + L-leucine
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Tyr-Leu + H2O
benzyloxycarbonyl-Tyr + L-leucine
show the reaction diagram
-
enzyme shows very low activity
-
-
?
bradykinin I + H2O
?
show the reaction diagram
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truncated KexA releases amino acid residues from the C terminus of bradykinin I
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-
?
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
show the reaction diagram
Dansyl-Phe-Ala-Arg + H2O
Dansyl-Phe-Ala + Arg
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
show the reaction diagram
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
show the reaction diagram
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-
-
?
[Leu5]enkephalin-Arg6 + H2O
?
show the reaction diagram
-
-
-
-
?
[Leu5]enkephalin-Lys6 + H2O
?
show the reaction diagram
-
-
-
-
?
[Met5]enkephalin-Arg6 + H2O
?
show the reaction diagram
-
-
-
-
?
[Met5]enkephalin-Lys6 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activates at low concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1-chloro-3-tosylamido-7-amino-2-heptanone
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4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
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alpha-Factor KR
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chymostatin
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pH 5.6, 50% inhibition at 13000 nM, pH 6.5, 50% inhibition at 2200 nM. Comparison with inhibitory effect on other peptidases
diisopropyl fluorophosphate
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
ebelactone B
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pH 5.6, 50% inhibition at 2100 nM, pH 6.5, 50% inhibition at 1500 nM. Comparison with inhibitory effect on other peptidases
Enkephalin heptapeptides
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Guanidinoethylmercaptosuccinic acid
lactacystin
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pH 5.6, 50% inhibition at 1400 nM, pH 6.5, 50% inhibition at 4300 nM. Comparison with inhibitory effect on other peptidases
monoiodo acetic acid
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90% inhibition
N-[N-(L-3-trans-carboxirane-2-carbonyl)-L-leucyl]-agmatine
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8% inhibition
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omuralide
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i.e. (1S,4S,5R)-1-[(1S)-1-hydroxy-2-methylpropyl]-4-methyl-6-oxa-2-azabicyclo[3.2.0]heptane-3,7-dione, pH 5.6, 50% inhibition at 4.8 nM, pH 6.5, 50% inhibition at 2 nM. Comparison with inhibitory effect on other peptidases
PCMB
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domain 1B and domain
phenylmethylsulfonyl fluoride
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PMSF
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68% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.284 - 0.335
Benzoyl-Phe-Ala-Arg
0.063 - 0.132
dansyl-L-Ala-L-Arg
0.208 - 0.246
dansyl-Phe-Ala-Arg
0.516
furylacryloyl-Ala-Arg
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-
0.962
furylacryloyl-Ala-Lys
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.86 - 32.6
dansyl-Phe-Ala-Arg
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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60 U/ml, purified truncated Kex-1-C611
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
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wild-type enzyme
6.3
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activity assay
6.5 - 7
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and 5.6. Activity maximum at pH 5.6 is due to activity of domain II, at pH 6.5-7.0 due to domain I
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
cleavage assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pI-value below pH 3.0
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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exclusive expression of 180 kDa isoform
Manually annotated by BRENDA team
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T-lymphoma cell, exclusive synthesis of isoform SPD-N
Manually annotated by BRENDA team
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lymphoma cell, exclusive synthesis of isoform SPD-N
Manually annotated by BRENDA team
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Schneider 2 cell line, each splice variant of enzyme occurs in this cell line. Short enzyme forms containing a single carboxypeptidase domain are secreted from S2 cells, while long forms containing three carboxypeptidase domains, a transmembrane domain, and one out of two cytosolic domains are retained. C-terminal tail 2 leads to Golgi localization. The two C-terminal tails result in different internalization efficiencies from the cell surface
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
98% of enzymic activity
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8700
-
gel filtration of the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL)
58000
-
calculated, truncated Kex-1-C611
58820
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truncated form, calculated from cDNA
67000
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determined by SDS-PAGE, truncated Kex-1-C611
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 54219, calculation from nucleotide sequence
monomer
-
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) is a monomer in solution
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of KEX1DELTAp, an enzyme form lacking the acidic and the membrane-spanning domain at 2.4 A resolution; structure of Kex1DELTAp, an enzyme that lacks the acidic domain and membrane-spanning portion of Kex1p
crystal structure at 2.2 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
-
731176
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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maximum temperature at which the enzyme has residual activity of over 60% relative to maximum activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
archieved by a two-step chromatographic process using cation-exchange, SP Sepharose, followed by anion-exchange, DEAE Sepharose FF resin
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domain 1B and 2 expressed in Sf9 cells using baculovirus expression system
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KEX1 gene from Saccharomyces cerevisiae expressed using the baculovirus/insect cell system
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using anion-exchange chromatography and gel filtration
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using IgG-Sepharose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a truncated form of Kex-1, Kex-1-C611, is constructed comprising the amino acid residues from 104-611 and lacks the transmembrane domain
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a truncated form of KexA (amino acid residues 1 to 526 of KexA), which lack the potential transmembrane region and the succeeding C-terminal sequence (amino acid residues 527 to 625 of KexA) is expressed by using a protein expression system with the pIECS3 vector and Aspergillus nidulans
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individual domains of the enzyme are expressed in insect Sf9 cells using the baculovirus expression system. Medium from domain 1B-expressing cells and domain 2-expressing cells shows substantial enzymatic activity, whereas medium from domain 1A-expressing cells is not different from cells infected with wild-type virus. The individual domains 1A, 1B, and 2 are expressed in baculovirus under the polyhedrin promoter and with the signal peptide of the rat enzyme
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into the yeast shuttle vector pVT100-ZZ
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the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (residues 386-460, h-TTL), is cloned into the pET-22B vector to encode a C-terminal hexahistidine fusion protein. Expression carried out in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CPD is upregulated in human HCC cell lines and tumor tissues
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testosterone and prolactin increase carboxypeptidase D mRNA expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E353Q
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cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 1
E771Q
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cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 2
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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Kex-1-C611 is proposed as a convenient biotechnological reagent for the cleavage of fusion proteins
molecular biology
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Kex2 and Kex1 may promote cell fusion by proteolytically processing substrates that act in parallel to Prm1 (pheromone-regulated membrane protein 1) as an alternative fusion machine, as cell wall components, or both
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