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

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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.16.5
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase C
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9046-67-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
cathepsin A is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human antigen-presenting cells
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
?
-
INHIBITORS
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, 27C
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, 27C
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, 37C
0.000057
(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000357
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000038
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000252
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000274
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
0.0001
(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000059
(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000087
(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
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, 37C
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, 37C
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, 37C
0.00011
(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.0001
(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.00007
(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
0.000015
(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.000015
(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
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, 37C
0.000226
3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
Homo sapiens;
-
pH 6, 37C
0.000026
3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
0.03
3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
0.0001
3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
Homo sapiens;
-
pH 6, 37C
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, 37C
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, 37C
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, 37C
0.0002
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
Homo sapiens;
-
pH 6, 37C
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
-
enzymatic activity increases with maturation of cathepsin A to the 51.1 kDa form
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
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
SDS-PAGE
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
100000
-
native complex, SDS-PAGE
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
somewhat unstable above at 37C
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
-
ENGINEERING
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