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Information on EC 3.4.16.5 - carboxypeptidase C and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.5 carboxypeptidase C
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
release of a C-terminal amino acid with broad specificity
Synonyms
carboxypeptidase y, cathepsin a, catha, deamidase, serine carboxypeptidase, protective protein/cathepsin a, scpep1, procpy, carboxypeptidase yscy, carboxypeptidase-y, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A-type metallocarboxypeptidase
-
-
carboxypeptidase A4
-
-
carboxypeptidase Y
carboxypeptidase YSCY
-
-
-
-
cathepsin A
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPA4
-
-
deamidase
-
-
-
-
EC 3.4.16.1
formerly
hCath A
-
-
lysosomal carboxypeptidase A
lysosomal protective protein
MO54
-
-
-
-
Phaseolin
-
-
-
-
protective protein/cathepsin A
-
serine carboxypeptidase I
-
-
-
-
additional information
-
this enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 3.4.16.3, not a homologue of chymotrypsin or subtilisin, see reference
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9046-67-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu-Arg + H2O
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu + Arg
show the reaction diagram
-
-
-
?
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine + H2O
?
show the reaction diagram
-
-
-
-
?
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Leu + H2O
benzyloxycarbonyl-L-Phe + L-Leu
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
CBZ-Phe-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-leucine
show the reaction diagram
-
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
show the reaction diagram
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
-
?
FVNQHLCGSHLV + H2O
FVNQHLCGSH + L-Leu-L-Val + L-Val
show the reaction diagram
-
-
-
-
?
FVNQHLCGSHLVEAL + H2O
FVNQHLCGSHLVE + L-Ala-L-Leu + L-Leu
show the reaction diagram
-
-
-
-
?
lysosomal neuraminidase-1 + H2O
?
show the reaction diagram
lysosomal neuraminidase-1 gains full catalytic activity in the lysosome through its binding to PPCA
-
-
?
N-(4-methoxyphenyl-azoformyl)-L-Phe-OH + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-[2-(trifluoromethyl)phenyl]propanoic acid
-
-
(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([4-chloro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([4-fluoro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
-
-
(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]-3-(2-methylphenyl)propanoic acid
-
-
3,4-dichloroisocoumarin
-
effective inhibitor
3-(([1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-fluorophenyl)propanoic acid
-
-
3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
-
-
3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
-
-
3-(2,3-dichlorophenyl)-3-(([1-(2,4-difluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
-
-
3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
-
-
3-(4'-fluorobiphenyl-4-yl)-3-([[1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
3-(5-fluoro-2-methylphenyl)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
-
-
3-(biphenyl-4-yl)-3-([[1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
-
-
benzyloxycarbonyl-Gly-Leu-Phe-CH2Cl
-
-
chymostatin
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
diisopropyl fluorophosphate
ebelactone B
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
lactacystin
omuralide
Phe-Asn-Arg-Ala-Val-Asp
-
-
Phe-Asn-Arg-Ala-Val-Val
-
-
Phe-Asn-Arg-Pro-Val-Asp
-
-
Phe-Asn-Arg-Pro-Val-Val
-
-
piperastatin A
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
additional information
-
not inhibited by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.363
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
0.61
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
0.04
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
237
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
1777
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
12.1
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078
(3R)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000057
(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000357
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000038
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000252
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000274
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000375
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-[2-(trifluoromethyl)phenyl]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000059
(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000087
(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00011
(3S)-3-(([4-chloro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00003
(3S)-3-(([4-fluoro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00006
(3S)-3-(2,4-dichlorophenyl)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000005 - 0.00005
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
0.00007
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00011
(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00007
(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000003
(3S)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000015
(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000015
(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00001
(3S)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0006
3,4-dichloroisocoumarin
Homo sapiens
-
-
0.00538
3-(([1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-fluorophenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000226
3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
Homo sapiens
-
pH 6, 37°C
0.000026
3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.03
3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00012
3-(2,3-dichlorophenyl)-3-(([1-(2,4-difluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000025
3-(4'-fluorobiphenyl-4-yl)-3-([[1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000076
3-(5-fluoro-2-methylphenyl)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000803
3-(biphenyl-4-yl)-3-([[1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0002
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.092 - 0.1
chymostatin
Homo sapiens
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
0.01
diisopropyl fluorophosphate
Homo sapiens
-
-
0.0016 - 0.002
ebelactone B
Homo sapiens
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
0.0018 - 0.0052
lactacystin
Homo sapiens
-
IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
0.000012 - 0.000099
omuralide
Homo sapiens
-
IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
0.72
Phe-Asn-Arg-Ala-Val-Asp
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.63
Phe-Asn-Arg-Ala-Val-Val
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.91
Phe-Asn-Arg-Pro-Val-Asp
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.71
Phe-Asn-Arg-Pro-Val-Val
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.018 - 0.032
piperastatin A
Homo sapiens
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
0.1
poststatin
Homo sapiens
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
assay at
5.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
27
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from a galactosialidosis patient transformed with simian virus-40-adenovirus recombinant
Manually annotated by BRENDA team
-
vascular
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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?
PPGB_HUMAN
480
0
54466
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
native complex, SDS-PAGE
29000
-
SDS-PAGE
32000
50000
-
proform, SDS-PAGE
51100
MALDI-TOF, mature protein. Enzymatic activity increases with maturation of Cathepsin A to the 51.1 kDa form
54000
proenzyme, SDS-PAGE
54400
MALDI-TOF, zymogen protein
additional information
-
overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
proteolytic modification
the activation of precursor cathepsin A is achieved by proteolytic removal of a larger 3.3-kDa peptide that includes the blocking peptide, bypassing the requirement for conformational changes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mature cathepsin A is determined to 2.8 A resolution
crystal structures show that the structure of mature Cathepsin A is identical to the structure of the precursor and that activation depends solely on the removal/disorder transition of the activation domain. The active catalytic domain is held together by a strategically located disulfide bridge, linking the loose ends that are formed after removal/disorder transition of the activation domain
sitting drop vapour diffusion method with 0.2 M potassium thiocyanate and 20% PEG 3350
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A251E
the mutant shows increased activity compared to the wild type cathepsin A
K355Q
the mutant shows increased activity compared to the wild type cathepsin A
L354D
the mutant shows decreased activity compared to the wild type cathepsin A
P451A
the mutant shows increased activity compared to the wild type cathepsin A
R20A
the mutant shows decreased activity compared to the wild type cathepsin A
R262A/R292A
double mutant also undergoes processing to form large and small subunits, suggesting alternative avenues for the maturation of cathepsin A
R344A
the mutant shows about wild type cathepsin A activity
R344D
inactive mutant, the 54 kDa precursor/zymogen with the R344D substitution is not processed to the 32/20 kDa mature form with CathA activity
R344E
the mutant shows reduced cathepsin A activity compared to the wild type
R344G
the mutant shows reduced cathepsin A activity compared to the wild type
R344I
the mutant shows reduced cathepsin A activity compared to the wild type
R344K
the mutant shows reduced cathepsin A activity compared to the wild type
R344M
the mutant shows reduced cathepsin A activity compared to the wild type
R344N
the mutant shows reduced cathepsin A activity compared to the wild type
R344P
the mutant shows reduced cathepsin A activity compared to the wild type
R344Q
the mutant shows reduced cathepsin A activity compared to the wild type
R344S
the mutant shows about wild type cathepsin A activity
R344V
the mutant shows reduced cathepsin A activity compared to the wild type
S150A/R284A/R298A
triple mutant S150A/R284A/R298A also undergoes cleavage into large and small subunits, comparable with the wildtype cathepsin A, suggesting that these sites are not mandatory for the activation of cathepsin A
W382A
the mutant shows decreased activity compared to the wild type cathepsin A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
somewhat unstable above at 37°C
647190
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified by metal-chelate and gel-filtration chromatography
Superdex S-200 gel filtration and HR Mono P column chromatography
-
TSK-DEAE 5PW column chromatography
-
using affinity and ion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a flagged tagged fusion protein in Tn5 insect cells
expressed in Escherichia coli as a His-tagged fusion protein
expressed in insect cells
expressed in Pichia pastoris
-
expressed in T-1 cells
overexpression in mouse and rat cardiomyocytes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackman, H.L.; Morris, P.W.; Deddish, P.A.; Skidgel, R.A.; Erds, E.G.
Inactivation of endothelin I by deamidase (lysosomal protective protein)
J. Biol. Chem.
267
2872-2875
1992
Homo sapiens
Manually annotated by BRENDA team
Breddam, K.
Serine carboxypeptidases. A review
Carlsberg Res. Commun.
51
83-128
1986
Saccharomyces cerevisiae, Citrus sp., Homo sapiens, Triticum aestivum
-
Manually annotated by BRENDA team
Aikawa, S.I.; Matsuzawa, F.; Satoh, Y.; Kadota, Y.; Doi, H.; Itoh, K.
Prediction of the mechanism of action of omuralide (clasto-lactacystin beta-lactone) on human cathepsin A based on a structural model of the yeast proteasome beta5/PRE2-subunit/omuralide complex
Biochim. Biophys. Acta
1764
1372-1380
2006
Homo sapiens
Manually annotated by BRENDA team
Satoh, Y.; Kadota, Y.; Oheda, Y.; Kuwahara, J.; Aikawa, S.; Matsuzawa, F.; Doi, H.; Aoyagi, T.; Sakuraba, H.; Itoh, K.
Microbial serine carboxypeptidase inhibitors. Comparative analysis of actions on homologous enzymes derived from man, yeast and wheat. [Erratum to document cited in CA142:109255]
J. Antibiot.
57
316-325
2004
Saccharomyces cerevisiae, Homo sapiens, Triticum aestivum
Manually annotated by BRENDA team
Birkus, G.; Wang, R.; Liu, X.; Kutty, N.; MacArthur, H.; Cihlar, T.; Gibbs, C.; Swaminathan, S.; Lee, W.; McDermott, M.
Cathepsin A is the major hydrolase catalyzing the intracellular hydrolysis of the antiretroviral nucleotide phosphonoamidate prodrugs GS-7340 and GS-9131
Antimicrob. Agents Chemother.
51
543-550
2007
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
Manually annotated by BRENDA team
Yoshida, T.; Kadota, Y.; Hitaoka, S.; Kori, E.; Horikawa, Y.; Taguchi, M.; Tsuji, D.; Hirokawa, T.; Chuman, H.; Itoh, K.
Expression and molecular dynamics studies on effect of amino acid substitutions at Arg344 in human cathepsin A on the protein local conformation
Biochim. Biophys. Acta
1794
1693-1699
2009
Homo sapiens (P10619), Homo sapiens
Manually annotated by BRENDA team
Reich, M.; Spindler, K.D.; Burret, M.; Kalbacher, H.; Boehm, B.O.; Burster, T.
Cathepsin A is expressed in primary human antigen-presenting cells
Immunol. Lett.
128
143-147
2010
Homo sapiens
Manually annotated by BRENDA team
Bonten, E.J.; Campos, Y.; Zaitsev, V.; Nourse, A.; Waddell, B.; Lewis, W.; Taylor, G.; dAzzo, A.
Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization
J. Biol. Chem.
284
28430-28441
2009
Homo sapiens (P10619)
Manually annotated by BRENDA team
Schreuder, H.A.; Liesum, A.; Kroll, K.; Boehnisch, B.; Buning, C.; Ruf, S.; Sadowski, T.
Crystal structure of cathepsin A, a novel target for the treatment of cardiovascular diseases
Biochem. Biophys. Res. Commun.
445
451-456
2014
Homo sapiens (P10619)
Manually annotated by BRENDA team
Kolli, N.; Garman, S.C.
Proteolytic activation of human cathepsin A
J. Biol. Chem.
289
11592-11600
2014
Homo sapiens (P10619), Homo sapiens
Manually annotated by BRENDA team
Ruf, S.; Buning, C.; Schreuder, H.; Horstick, G.; Linz, W.; Olpp, T.; Pernerstorfer, J.; Hiss, K.; Kroll, K.; Kannt, A.; Kohlmann, M.; Linz, D.; Huebschle, T.; Ruetten, H.; Wirth, K.; Schmidt, T.; Sadowski, T.
Novel beta-amino acid derivatives as inhibitors of cathepsin A
J. Med. Chem.
55
7636-7649
2012
Homo sapiens
Manually annotated by BRENDA team
Petrera, A.; Kern, U.; Linz, D.; Gomez-Auli, A.; Hohl, M.; Gassenhuber, J.; Sadowski, T.; Schilling, O.
Proteomic profiling of cardiomyocyte-specific cathepsin A overexpression links cathepsin A to the oxidative stress response
J. Proteome Res.
15
3188-3195
2016
Homo sapiens (P10619), Homo sapiens
Manually annotated by BRENDA team