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Information on EC 3.4.17.1 - carboxypeptidase A and Organism(s) Homo sapiens and UniProt Accession Q9UI42

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.1 carboxypeptidase A
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9UI42 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cpa, carboxypeptidase a, mcp-2, mc-cpa, carboxypeptidase a1, carboxypeptidase a3, carboxypeptidase-a, mast cell carboxypeptidase a, carboxypeptidase a4, mecpa, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A-type metallocarboxypeptidase
-
carboxypeptidase a
-
carboxypeptidase A4
-
Anson's enzyme
-
formerly
ASPA
-
-
aspartoacyclase
-
-
carboxypeptidase a
-
-
Carboxypeptidase A3
carboxypeptidase A4
-
-
carboxypeptidase vitellogenic-like
-
-
carboxypeptidase-A
-
-
carboxypolypeptidase
-
-
-
-
colon mast cell carboxypeptidase
-
-
CPVL
-
-
mast cell carboxypeptidase A
-
MC-CP
-
-
MC-CPA
Nna1/CCP1
-
-
PTD012
-
-
RMC-CP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
11075-17-5
-
9031-98-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-(4-methoxyphenyl-azoformyl)-L-Phe + H2O
?
show the reaction diagram
-
-
-
?
Phe-Asn-Arg-Pro-Val + H2O
?
show the reaction diagram
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Asp + H2O
?
show the reaction diagram
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Val + H2O
?
show the reaction diagram
used as substrate in the activity assay
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Ala + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ala
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Ile + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ile
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Leu + H2O
3-(2-furyl)acryloyl-L-Phe + L-Leu
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Met + H2O
3-(2-furyl)acryloyl-L-Phe + L-Met
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Phe + H2O
3-(2-furyl)acryloyl-L-Phe + L-Phe
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Trp + H2O
3-(2-furyl)acryloyl-L-Phe + L-Trp
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Val + H2O
3-(2-furyl)acryloyl-L-Phe + L-Val
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
?
show the reaction diagram
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
show the reaction diagram
-
-
-
-
?
apoB-100 + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein B + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + ?
show the reaction diagram
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
show the reaction diagram
-
-
-
ir
beta-actin (169-177) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
big SAAS + H2O
?
show the reaction diagram
-
good substrate
-
-
?
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carboxypeptidase A5 C-terminus + H2O
?
show the reaction diagram
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
cathepsin D (138-155) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
chromogranin A (374-388) + H2O
?
show the reaction diagram
-
good substrate
-
-
?
chromogranin A (374-390) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
chromogranin B + H2O
?
show the reaction diagram
-
good substrate
-
-
?
clathrin light chain A C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
des-Asp1-angiotensin + H2O
?
show the reaction diagram
-
partially cleaved in 2 h
-
-
?
dynorphin A8 + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
elongation factor 1 beta 2 N-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
endothelin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
ET-1 + H2O
?
show the reaction diagram
-
-
-
-
?
gamma-actin + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
Gly-L-Tyr + H2O
Gly + L-Tyr
show the reaction diagram
-
slow substrate
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
-
-
-
?
kinetensin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
?
show the reaction diagram
-
partially cleaved in 2 h
-
-
?
Leu5-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
little SAAS + H2O
?
show the reaction diagram
-
small percentage of cleavage
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
Met-enkephalin-L-Arg-L-Phe + H2O
Met-enkephalin-L-Arg + L-Phe
show the reaction diagram
-
-
-
-
?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
show the reaction diagram
-
low activity
-
-
?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
-
high activity
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
N-(4-methoxyphenylazoformyl)-Phe + H2O
?
show the reaction diagram
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe-OH + H2O
?
show the reaction diagram
-
substrate for inhibition assay
-
-
?
N-(methoxyphenyl-azoformyl)-Phe-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-aspartate
acetate + L-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-phenylalanyl-L-3-thiaphenylalanine + H2O
?
show the reaction diagram
-
assay substrate
-
-
?
N-[3-(2-furyl)acryloyl]-Phe-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
neuromedin N + H2O
?
show the reaction diagram
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
O-(trans-4-chlorocinnamoyl)-L-phenyllactic acid + H2O
trans-4-chlorocinnamic acid + L-phenyllactic acid
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
nitrophenolate + acetate
show the reaction diagram
-
-
-
-
?
peptidylprolyl isomerase A (118-129) + H2O
?
show the reaction diagram
-
good substrate
-
-
?
peptidylprolyl isomerase A (23-39) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (26-39) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-100) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-92) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peroxiredoxin V N-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
procholecystokinin (46-62) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
procholecystokinin (46-63) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
proenkenphalin octapeptide + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
proenkephalin + H2O
?
show the reaction diagram
-
good substrate
-
-
?
propeptidyl-amidating monooxygenase + H2O
?
show the reaction diagram
-
good substrate
-
-
?
proteasome subunit beta type 6 (34-41) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
protein PEN + H2O
?
show the reaction diagram
-
good substrate
-
-
?
protein PEN-20 + H2O
?
show the reaction diagram
-
good substrate
-
-
?
provasopressin (151-end) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
ribosomal protein S21 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
sarafotoxin + H2O
?
show the reaction diagram
-
-
-
-
?
sarafotoxin 6b + H2O
?
show the reaction diagram
-
-
-
-
?
secretogranin (287-316) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
secretogranin (300-316) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
snake venom toxin + H2O
?
show the reaction diagram
-
-
-
-
?
synaptosomal-associated protein C-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
thioredoxin N-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
vacuolar ATP synthase subunit 2 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
vasoconstrictive factor endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
voltage-dependent anion channel protein 1 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
xenopsin + H2O
?
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
angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein B + H2O
?
show the reaction diagram
-
-
-
-
?
endothelin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
kinetensin + H2O
?
show the reaction diagram
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
-
prodrug activation in SW122 cells
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
sarafotoxin 6b + H2O
?
show the reaction diagram
-
-
-
-
?
snake venom toxin + H2O
?
show the reaction diagram
-
-
-
-
?
vasoconstrictive factor endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
xenopsin + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
zinc enzyme, the zinc coordination number is five in the complex with the inhibitor 4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid and the resulting geometry is tetrahedral
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Gly-Asn-Arg-Pro-Thr
-
Gly-Asn-Arg-Pro-Val-Thr
-
Phe-Asn-Arg-Ala-Val-Asp
-
Phe-Asn-Arg-Ala-Val-Val
-
Phe-Asn-Arg-Pro-Val
-
Phe-Asn-Arg-Pro-Val-Asp
-
Phe-Asn-Arg-Pro-Val-Val
-
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(R)-N-sulfamoylphenylalanine
-
competitive
(R,S)-3-phenyl-2-sulfamoyloxypropionic acid
-
competitive
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
competitive
(R,S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R,S)-N-sulfamoylphenylalanine
-
competitive
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(S)-N-sulfamoylphenylalanine
-
competitive
1,10-phenanthroline
2-benzyl-3,4-epithiobutanoic acid
-
-
2-benzyl-3,4-epoxybutanoic acid
-
-
4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid
mechanism-based inhibitor
8-hydroxyquinoline
-
-
Ascaris carboxypeptidase inhibitor
-
-
-
Benzylsuccinic acid
DL-benzylsuccinic acid
-
-
endoglycosidase H
-
lowers CPVL expression in monocyte-derived macrophages
-
latexin
-
leech carboxypeptidase inhibitor
-
N-glycosidase
-
lowers CPVL expression in monocyte-derived macrophages
-
potato carboxypeptidase inhibitor
-
SR48692
-
-
tick carboxypeptidase inhibitor
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trypsin
activates zymogen
-
phorbol myristate acetate
-
-
proteoglycan
-
there is evidence indicating that the processing of pro-MC-CPA into active protease is dependent on proteoglycan
-
Trypsin
-
additional information
-
lipopolysaccharide has no effect on expression in monocyte-derived dendritic cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.372
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0233
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0194
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.04
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0556
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0615
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.0573
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.227
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.1
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
0.2
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
0.23 - 10
benzoyl-Gly-L-Phe
3 - 13.3
carbobenzoxy-Gly-L-Phe
0.075
hippuryl-L-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
0.165
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.55
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.00923
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.065
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25°C, recombinant enzyme
0.0043
methotrexate-alpha-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
0.000329
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.3
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
12.4
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
13.4
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
23.9
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
44.3
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
57.3
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
19.4
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
8.23
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
767
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
13.3
benzoyl-Gly-Gly-L-Phe
-
-
505
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
11.7 - 66.7
benzoyl-Gly-L-Phe
48.3 - 112
carbobenzoxy-Gly-L-Phe
4.3
hippuryl-L-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
2.33
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
3.43
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
1.45
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.09
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25°C, recombinant enzyme
1.9
methotrexate-alpha-phenylalanine
-
pH 7.4, 25°C, recombinant enzyme
0.24
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
0.042
p-nitrophenyl acetate
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
532
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
693
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
581
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
797
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
93
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
338
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
36
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
14
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
6.2
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
157
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
730
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.039
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.00209
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
pH 7.5
0.0032
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
1.9
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.0000239
Ascaris carboxypeptidase inhibitor
-
-
-
0.000003
latexin
-
0.0000073
leech carboxypeptidase inhibitor
-
-
-
0.0000013
potato carboxypeptidase inhibitor
-
-
-
0.0000008
tick carboxypeptidase inhibitor
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
Gly-Asn-Arg-Pro-Thr
Homo sapiens
-
0.72
Phe-Asn-Arg-Ala-Val-Asp
Homo sapiens
-
0.63
Phe-Asn-Arg-Ala-Val-Val
Homo sapiens
-
4 - 5
Phe-Asn-Arg-Pro-Val
0.91
Phe-Asn-Arg-Pro-Val-Asp
Homo sapiens
-
0.71
Phe-Asn-Arg-Pro-Val-Val
Homo sapiens
-
0.056
4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid
Homo sapiens
pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.7
-
recombinant enzyme secreted from Pichia pastoris, cell-free supernatant
7.2
-
purified recombinant enzyme, substrate hippuryl-L-phenylalanine
850
-
purified recombinant enzyme, substrate hippuryl-L-phenyllactate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
activity assay
7 - 9
-
-
7.4
-
assay at
7.5 - 8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.9
-
-
6 - 9.5
-
pH 6.0: about 25% of maximum activity, pH 9.5: about 70% of maximum activity
8.5 - 9
-
the optimal pH for cleavage of 3-(2-furyl)acryloyl-L-Phe-L-Phe and 3-(2-furyl)acryloyl-L-Phe-L-Ala is in the range of 8.5-9.0 with very low activity below pH 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
liver cancer cell line, high expression level
Manually annotated by BRENDA team
-
mast cell
Manually annotated by BRENDA team
-
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
in primary macrophages, CPVL is glycosylated with high mannose residues
Manually annotated by BRENDA team
-
CPVL is up-regulated during the maturation of monocytes to macrophages. Expression in monocyte-derived dendritic cells
Manually annotated by BRENDA team
-
PC-3m human prostate cancer cell line
Manually annotated by BRENDA team
-
antigen A33-prositive colon carcinoma cell line
Manually annotated by BRENDA team
-
expressed in phorbol myristate acetate-stimulated cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
present in ruffles of macrophages, absent from outer plasma membrane
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPA4_HUMAN
421
0
47351
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
-
Western blot analysis
34000
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
35000
-
gel filtration
35780
-
mature enzyme after cleavage of the signal- and activation peptides
36000
37000
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
38000
-
native ASPA expessed in COS-7 cells, determined by immunoblotting
42000
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
47140
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
48730
-
calculated from amino acid sequence
52000
-
recombinant human ASPA fused to N-terminal thioredoxin and C-terimal V5 and a 6x-histidine tag, analyzed by SDS-PAGE
80000
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
in solution, crystallography
additional information
-
amino acid composition described
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CPA4-hexapeptide complex crystallized by sitting drop vapor diffusion method, to 1.6 A resolution
structural details of a true cleaved double-product complex with a hexapeptide of human ocarboxypeptidase A4 employing diffraction data to 1.6 A resolution are provided
at 1.7 A resolution, structure is organized into a four-layer alphabetabetaalpha topology, zinc ion residing between the central beta-sheets is partially coordinated by three histidine residues
-
in complex with 2-benzyl-3,4-epithiobutanoic acid, hanging drop vapor diffusion method, using 20% PEG (w/v) 3350, 0.2 M NH4Cl, 0.02 M Tris pH 7.0
-
in complex with inhibitor 4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid
purified recombinant CPA4 in complex with latexin, hanging drop vapour diffusion method, 0.001 ml of 7 mg/ml protein solution is mixed with 0.001 ml reservoir solution containing 40% 2-methyl-2,4-pentanediol, 0.1 M [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)methane, pH 6.5, and with 0.002 ml 40% acetone, 20°C, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A305E
-
tested Canavan Disease mutation, results in undetectable enzyme activity
A57T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
C124A
-
alanine substitution of Cys124, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152A
-
alanine substitution of Cys152, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152W
-
tested Canavan Disease mutation, results in undetectable enzyme activity
C61A
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61S
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61W
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D204H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D249V
-
tested Canavan Disease mutation, results in undetectable enzyme activity
D68A
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E178A
-
mutation of the general proton donor
E214X
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E24D
-
mutation of a putative zinc-binding residue
E24G
-
mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity
E24H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
E24H/H116E
-
mutant designed to switch the order of the zinc-binding residues
E285A
-
tested Canavan Disease mutation
F295S
-
untested Canavan Disease mutation, results in undetectable enzyme activity
G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
H116E
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
H116G
-
mutation of a putative zinc-binding residue
H21E/E24H
-
mutant designed to switch the order of the zinc-binding residues
H21G
-
mutation of a putative zinc-binding residue
H21P
-
untested Canavan Disease mutation, results in undetectable enzyme activity
I143T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
K213E/G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
M195R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
P183H
-
untested Canavan Disease mutation
R127A
-
the mutation causes kcat to decrease from 12 to 0.012 which corresponds to a 6 kcal/mol decrease in the stabilization of transition state in the rate determining step
R63N
-
mutation that affects transition state stabilization
R71N
-
mutation that affects substrate carboxyl binding
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
completely inactive at pH 5
36329
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
50 min, 90% loss of activity
60
-
half-life of purified recombinant CPA2 is 24 min, and 8fold longer than for CPA1
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
effect of ionic strength: marked decrease of activity above 150 mM NaCl
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion-exchange chromatography
the active protein is obtained through tryptic activation, the resulting protein-product complex is subsequently purified by anion-exchange chromatography
by gel filtration and on anion-exchange column
-
purified with GST affinity chromatography
-
recombinant maltose binding protein-fusion enzyme from Escherichia coli by amylose affinity chromatography, digestion with thrombin, and heparin affinity chromatography
-
recombinant pro-CPA1 from Saccharomyces cerevisiae by anion exchange and hydrophobic interaction chromatography and another step of anion exchange chromatography followed by dialsis and gel filtration, to homogeneity
-
to more than 80% purity
-
TSK DEAE 5PW column chromatography
-
using nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
hCPA4 is produced as a zymogen through recombinant heterologous overexpression using vector pPIC9 and the methylotrophic yeast Pichia pastoris
produced as a zymogen through recombinant heterologous overexpression using vector pPIC9 and the methylotrophic yeast Pichia pastoris as expression host
a gamma-SmscFv/hCPA fusion protein is constructed, the pGEX-4T-1 and pUC19 vectors are used, recombinant proteins are expressed in Escherichia coli DH5alpha cells
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli as maltose binding protein-fusion protein with low activity level, methanol-inducible expression in Pichia pastoris with a high activity of the secreted recombinant enzyme
-
DNA and amino acid sequence determination and analysis, expression of the pro-CPA1 in Saccharomyces cerevisiae
-
DNA and amino acid sequence determination and analysis, the gene contains 11 exons and is located on chromosome 3, genetic organization, phylogenetic analysis
expressed in Pichia pastoris
-
expression of CPA4 in Pichia pastoris, scecretion of the recombinant enzyme to the culture medium
-
full-length human ASPA cDNA is subcloned into the pcDNA3.1/V5-His-TOPO vector, for bacterial expression mutants are generated directly in the pBAD/Thio-TOPO vector
-
into vector pET-28a(+) and expressed in Escherichia coli BL21-DE3 cells. BALB/c mice inoculated subcutaneously with recombinant CPVL. CHO cells transiently transfected with CPVL-EGFP expression vector
-
into vector pQTEV and introduced into Escherichia coli SCS1 cells carrying pRARE. The resulting clone used for expression of unlabeled protein. For expression of selenomethionine-labeled protein, the plasmid used to transform B834 Escherichia coli cells
-
subcloned into pcDNA3 lacking the KpnI site. MYPYDVPDYA ligated into the KpnI site of CCP1, which is located in the C-terminal region following the carboxypeptidase domain. Expression in Neuro2A and NIH3T3 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CPA4 is upregulated by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells
-
MC-CPA gene expression is about 2fold upregulated by bacterial lipopolysaccharide
-
TH2-high asthma cells are characterized by expression of CPA3
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
engaged in prostate cancer
analysis
the enzyme can serve as specific molecular maker for mast cells amongst normal hematopoietic cell populations
medicine
additional information
-
PTD012 might not belong to the carboxypeptidase family of enzymes, might belong to the superfamily of metallo-beta-lactamase fold proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riordan, J.F.; Holmquist, B.
Carboxypeptidase A
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
44-55
1984
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Appel, W.
Carboxypeptidasen
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
1023-1037
1974
Bos taurus, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Peterson, L.M.; Sokolovsky, M.; Vallee, B.L.
Purification and crystallization of human carboxypeptidase A
Biochemistry
15
2501-2508
1976
Homo sapiens
Manually annotated by BRENDA team
Park, J.D.; Kim, D.H.
Sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A
Bioorg. Med. Chem.
12
2349-2356
2004
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Laethem, R.M.; Blumenkopf, T.A.; Cory, M.; Elwell, L.; Moxham, C.P.; Ray, P.H.; Walton, L.M.; Smith, G.K.
Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2
Arch. Biochem. Biophys.
332
8-18
1996
Homo sapiens
Manually annotated by BRENDA team
Deckert, P.M.; Bornmann, W.G.; Ritter, G.; Williams, C.; Franke, J.; Keilholz, U.; Thiel, E.; Old, L.J.; Bertino, J.R.; Welt, S.
Specific tumour localisation of a huA33 antibody-carboxypeptidase A conjugate and activation of methotrexate-phenylalanine
Int. J. Oncol.
24
1289-1295
2004
Homo sapiens
Manually annotated by BRENDA team
Reynolds, D.S.; Gurley, D.S.; Austen, K.F.
Cloning and characterization of the novel gene for mast cell carboxypeptidase A
J. Clin. Invest.
89
273-282
1992
Homo sapiens (P15088), Homo sapiens
Manually annotated by BRENDA team
Dominguez-Munoz, J.E.; Martinez, S.M.; Leodolter, A.; Malfertheiner, P.
Quantification of pancreatic zinc output as pancreatic function test: making the secretin-caerulein test applicable to clinical practice
Pancreatology
4
57-62
2004
Homo sapiens
Manually annotated by BRENDA team
Pallares, I.; Bonet, R.; Garcia-Castellanos, R.; Ventura, S.; Aviles, F.X.; Vendrell, J.; Gomis-Rueth, F.X.
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin
Proc. Natl. Acad. Sci. USA
102
3978-3983
2005
Homo sapiens
Manually annotated by BRENDA team
Chen, Z.Q.; He, S.H.
Cloning and expression of human colon mast cell carboxypeptidase
World J. Gastroenterol.
10
342-347
2004
Homo sapiens
Manually annotated by BRENDA team
Bayes, A.; Fernandez, D.; Sola, M.; Marrero, A.; Garcia-Pique, S.; Aviles, F.X.; Vendrell, J.; Gomis-Rueth, F.X.
Caught after the act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide
Biochemistry
46
6921-6930
2007
Homo sapiens (Q9UI42), Homo sapiens
Manually annotated by BRENDA team
Hershfield, J.R.; Pattabiraman, N.; Madhavarao, C.N.; Namboodiri, M.A.
Mutational analysis of aspartoacylase: implications for Canavan disease
Brain Res.
1148
1-14
2007
Homo sapiens
Manually annotated by BRENDA team
Pejler, G.; Aabrink, M.; Ringvall, M.; Wernersson, S.
Mast cell proteases
Adv. Immunol.
95
167-255
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Matsugi, S.; Hamada, T.; Shioi, N.; Tanaka, T.; Kumada, T.; Satomura, S.
Serum carboxypeptidase A activity as a biomarker for early-stage pancreatic carcinoma
Clin. Chim. Acta
378
147-153
2007
Homo sapiens
Manually annotated by BRENDA team
Bernkop-Schnuerch, A.; Schmitz, T.
Presystemic metabolism of orally administered peptide drugs and strategies to overcome it
Curr. Drug Metab.
8
509-517
2007
Homo sapiens
Manually annotated by BRENDA team
Yanes, O.; Nazabal, A.; Wenzel, R.; Zenobi, R.; Aviles, F.X.
Detection of noncovalent complexes in biological samples by intensity fading and high-mass detection MALDI-TOF mass spectrometry
J. Proteome Res.
5
2711-2719
2006
Homo sapiens
Manually annotated by BRENDA team
Hao, X.K.; Liu, J.Y.; Yue, Q.H.; Wu, G.J.; Bai, Y.J.; Yin, Y.
In vitro and in vivo prodrug therapy of prostate cancer using anti-gamma-Sm-scFv/hCPA fusion protein
Prostate
66
858-866
2006
Homo sapiens
Manually annotated by BRENDA team
Kalinina, E.; Biswas, R.; Berezniuk, I.; Hermoso, A.; Aviles, F.X.; Fricker, L.D.
A novel subfamily of mouse cytosolic carboxypeptidase
FASEB J.
21
836-850
2007
Homo sapiens, Mus musculus, Mus musculus C57B6
Manually annotated by BRENDA team
Harris, J.; Schwinn, N.; Mahoney, J.A.; Lin, H.; Shaw, M.; Howard, C.J.; da Silva, R.P.; Gordon, S.
A vitellogenic-like carboxypeptidase expressed by human macrophages is localized in endoplasmic reticulum and membrane ruffles
Int. J. Exp. Pathol.
87
29-39
2006
Candida albicans, Homo sapiens
Manually annotated by BRENDA team
Manjasetty, B.A.; Buessow, K.; Fieber-Erdmann, M.; Roske, Y.; Gobom, J.; Scheich, C.; Goetz, F.; Niesen, F.H.; Heinemann, U.
Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold
Protein Sci.
15
914-920
2006
Homo sapiens
Manually annotated by BRENDA team
Fernandez, D.; Testero, S.; Vendrell, J.; Aviles, F.X.; Mobashery, S.
The X-ray structure of carboxypeptidase A inhibited by a thiirane mechanism-based inhibitor
Chem. Biol. Drug Des.
75
29-34
2010
Homo sapiens
Manually annotated by BRENDA team
Dougherty, R.H.; Sidhu, S.S.; Raman, K.; Solon, M.; Solberg, O.D.; Caughey, G.H.; Woodruff, P.G.; Fahy, J.V.
Accumulation of intraepithelial mast cells with a unique protease phenotype in TH2-high asthma
J. Allergy Clin. Immunol.
125
1046-1053
2010
Homo sapiens
Manually annotated by BRENDA team
Tanco, S.; Zhang, X.; Morano, C.; Aviles, F.X.; Lorenzo, J.; Fricker, L.D.
Characterization of the substrate specificity of human carboxypeptidase A4 and implications for a role in extracellular peptide processing
J. Biol. Chem.
285
18385-18396
2010
Homo sapiens
Manually annotated by BRENDA team
Van Damme, P.; Staes, A.; Bronsoms, S.; Helsens, K.; Colaert, N.; Timmerman, E.; Aviles, F.X.; Vandekerckhove, J.; Gevaert, K.
Complementary positional proteomics for screening substrates of endo- and exoproteases
Nat. Methods
7
512-515
2010
Homo sapiens
Manually annotated by BRENDA team
Kilshtain, A.V.; Warshel, A.
On the origin of the catalytic power of carboxypeptidase A and other metalloenzymes
Proteins
77
536-550
2009
Homo sapiens
Manually annotated by BRENDA team
Pejler, G.; Knight, S.D.; Henningsson, F.; Wernersson, S.
Novel insights into the biological function of mast cell carboxypeptidase A
Trends Immunol.
30
401-408
2009
Homo sapiens
Manually annotated by BRENDA team
Testero, S.A.; Granados, C.; Fernandez, D.; Gallego, P.; Covaleda, G.; Reverter, D.; Vendrell, J.; Aviles, F.X.; Pallares, I.; Mobashery, S.
Discovery of mechanism-based inactivators for human pancreatic carboxypeptidase A from a focused synthetic library
ACS Med. Chem. Lett.
8
1122-1127
2017
Homo sapiens (P15085), Homo sapiens
Manually annotated by BRENDA team
Zhang, H.; Hao, C.; Wang, H.; Shang, H.; Li, Z.
Carboxypeptidase A4 promotes proliferation and stem cell characteristics of hepatocellular carcinoma
Int. J. Exp. Pathol.
100
133-138
2019
Homo sapiens
Manually annotated by BRENDA team