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Information on EC 3.4.16.5 - carboxypeptidase C and Organism(s) Homo sapiens and UniProt Accession P10619

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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
UNIPROT: P10619 not found.
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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
carboxypeptidase Y
-
EC 3.4.16.1
formerly
lysosomal protective protein
-
protective protein/cathepsin A
-
A-type metallocarboxypeptidase
-
-
carboxypeptidase A4
-
-
carboxypeptidase Y
-
-
-
-
carboxypeptidase YSCY
-
-
-
-
cathepsin A
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPA4
-
-
CPY
-
-
-
-
deamidase
-
-
-
-
hCath A
-
-
lysosomal carboxypeptidase A
lysosomal protective protein
-
-
-
-
MO54
-
-
-
-
Phaseolin
-
-
-
-
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
benzyloxycarbonyl-L-Phe-L-Leu + H2O
benzyloxycarbonyl-L-Phe + L-Leu
show the reaction diagram
-
-
-
?
CBZ-Phe-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-leucine
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
-
-
?
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-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
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
-
-
-
-
?
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
0.04
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
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
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.1
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
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
-
-
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
27
assay at
20
-
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
mouse model of cardiomyocyte-specific human CTSA overexpression. CTSA strongly impairs the balance of the proteolytic system by upregulating proteases such as cathepsin B, cathepsin D, and cathepsin Z while downregulating numerous protease inhibitors. Cardiomyocyte-specific human CTSA overexpression strongly reduces the levels of numerous antioxidative stress proteins, i.e., peroxiredoxins and protein deglycase DJ-1. In vitro, using cultured rat cardiomyocytes, ectopic overexpression of CTSA results in accumulation of reactive oxygen species
physiological function
-
cathepsin A is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human antigen-presenting cells
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
32000
mature enzyme, 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
100000
-
native complex, SDS-PAGE
29000
-
SDS-PAGE
32000
-
mature form, SDS-PAGE
50000
-
proform, SDS-PAGE
additional information
-
overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
glycoprotein
-
-
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
using affinity and ion-exchange chromatography
Superdex S-200 gel filtration and HR Mono P column chromatography
-
TSK-DEAE 5PW column 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 T-1 cells
overexpression in mouse and rat cardiomyocytes
expressed in Pichia pastoris
-
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