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Information on EC 3.4.23.34 - cathepsin E and Organism(s) Homo sapiens and UniProt Accession P14091
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3.4.23.34 cathepsin ESpecify your search results
Word Map
- 3.4.23.34
- cathepsins
- proteinases
- pepstatin
- pepsinogen
-
procathepsin
- molecular biology
- gastricsin
- medicine
-
foveolar
-
non-lysosomal
-
3.4.23.5
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cathepsin e, cathepsin d-like acid proteinase, cathepsin d-like protease, slow-moving proteinase, slow moving proteinase, cathepsin e-like acid proteinase, non-pepsin proteinase, cathepsin d-like aspartic proteinase, gastric mucosa non-pepsin acid proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CatE
Cathepsin D-like acid proteinase
-
-
-
-
Cathepsin D-type proteinase
-
-
-
-
Cathepsin E-like acid proteinase
-
-
-
-
EMAP
-
-
-
-
Erythrocyte membrane aspartic proteinase
-
-
-
-
Non-pepsin proteinase
-
-
-
-
Slow-moving proteinase
-
-
-
-
SMP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
110910-42-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
most sensitive and selective substrate for cathepsin E. This substrate might represent a useful tool for monitoring and accurately quantifying cathepsin E, even in crude enzyme preparations
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide + H2O
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu + L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
due to the close proximity of a Mca-donor and a Dnp-acceptor, near complete intramolecular quenching effect is achieved in the substrate's intact state. After the proteolytic cleavage of the hydrophobic motif, both Mca and Dnp are further apart, resulting in bright fluorescence
substrate shows a 265fold difference in the net fluorescence signals between cathepsins E and D. This cathepsin E selectivity is established by having Leu-Pro residues at the scissile peptide bond
-
?
DED-[5-[(2-aminoethyl)amino]naphthalene-1-sulfonyl]-KPILFFRLGK-[4-(4-dimethylaminophenylazo)benzoic acid] + H2O
?
-
-
-
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
Human endothelin precursor big ET-2 + H2O
Human endothelin precursor ET-2 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-3 + H2O
Huamn endothelin precursor ET-3 + respective C-terminal fragment
-
cleavage site: Trp-Ile
-
?
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
-
-
-
?
MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(DNP)-D-Arg-NH2 + H2O
hydrolyzed MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(DNP)-D-Arg-NH2
-
-
-
-
?
Reduced and carboxymethylated bovine pancreatic ribonuclease A + H2O
Hydrolyzed bovine pancreatic RCm ribonuclease A
-
-
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, best peptide substrate, cleavage site: Phe-Phe
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide, less suitable peptide substrate than substance P or other tachykinins
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
pH 7.4
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
no activation by ATP
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
no activation by ATP
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage specificity changes significantly with pH, e.g. cleaves Glu13-Ala14 only at pH 7.4
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
-
?
additional information
?
-
-
no hydrolysis of synthetic peptides corresponding to residues His16-His27 and His16-Ser38 in the big ET-1 sequence
-
-
?
additional information
?
-
-
milk-clotting activity is twice as high as that of pepsinogen and gastricin
-
-
?
additional information
?
-
-
degradation of protein antigens, crucial step in the initiation of a T-cell mediated immune response
-
?
additional information
?
-
-
cathepsin E has an important role in the class II MHC Ag processing pathway within dendritic cells
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
degradation of protein antigens, crucial step in the initiation of a T-cell mediated immune response
-
?
additional information
?
-
-
cathepsin E has an important role in the class II MHC Ag processing pathway within dendritic cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
-
i.e. H-77, with reduced isostere as replacement of the-CO-NH- of the peptide bond
alpha2-Macroglobulin
-
at pH 5.5, RNAse as substrate, at a molar ratio of enzyme/inhibitor of 0.5:1 to 2:1, above a ratio of 2:1 the excess enzyme is not inhibited, structural changes in alpha2-macroglobulin upon complex formation, no inhibition with oxidized insulin B-chain as substrate
-
grassystatin A
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin B
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin C
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
-
i.e. H-261, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Phe-Arg-Glu
-
i.e. H-256, with reduced isostere as replacement of the -CO-NH- of the peptide bond
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
-
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
i.e. L-363,564, hemoglobin as substrate
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
-
i.e. H-297, with reduced isostere as replacement of the -CO-NH- of the peptide bond
additional information
-
inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
-
additional information
-
inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
-
additional information
-
iodoaceteic acid, EDTA, phosphoramidon on proteolysis of membrane proteins
-
additional information
-
1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4)
-
additional information
-
1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4)
-
additional information
-
the computed three-dimensional structure of cathepsin-E and the relevant findings might provide useful insights for designing inhibitors with the desired selectivity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-(4-chlorophenyl)imidazo[2,1-b]thiazole-5-carbaldehyde O-(3,4-dichlorobenzyl)oxime
-
CITCO
additional information
-
the catalytically inactive proenzyme procathepsin E is rapidly converted to the active enzyme cathepsin E after brief treatment at pH 4 by autoproteolytic cleavage at Met36-Ile37 and Phe39-Thr40 to form two mature isozymic forms
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, erythrocyte cathepsin E
1.94
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
pH 4.0, 27°C
0.0068
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
25°C, pH 4.0
0.04
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
additional information
additional information
-
recombinant enzyme is catalytically indistinguishable from natural cathepsin
-
additional information
additional information
-
kinetic parameters of peptide hydrolysis of cathepsin E and pepsin
-
additional information
additional information
-
apparent Km-values of hemoglobin hydrolysis
-
additional information
additional information
-
apparent Km-values of hemoglobin hydrolysis
-
additional information
additional information
-
pH-dependence of kinetic constants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.4
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, erythrocyte cathepsin E
322.5
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
pH 4.0, 27°C
82
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
Cys4-Ala mutant cathepsin E, pH 3.1
11
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 6.6 and without ATP, pH 5
70
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
Cys4-Ala mutant cathepsin E, pH 3.1
additional information
additional information
-
pH-dependence of kinetic constants
-
additional information
additional information
-
pH-dependence of kinetic constants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
167
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
pH 4.0, 27°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000145
Ascaris pepsin inhibitor
-
40°C, pH 4.0, erythrocyte cathepsin E, hydrolysis of (7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
0.0000084
pepstatin A
-
40°C, pH 4.0, erythrocyte cathepsin E, hydrolysis of (7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no difference with respect to pH-dependence of hydrolysis between recombinant and native enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 4
-
90% of maximal activity at pH 2 and half-maximal activity at pH 4, hemoglobin as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
pancreas from normal, chronic pancreatitis and pancreatic ductal adenocarcinoma patients
-
-
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
immunocytochemical localization of recombinant enzyme in transfected cells
-
-
in different cell types such as gastric epithelial cells, Langerhans cells, interdigitating reticulum cell and human M cells
-
in antigen-presenting cells such as microglia, dendritic cells and macrophagess CatE is mainly present in the endosomal compartments
-
in different cell types such as gastric epithelial cells, Langerhans cells, interdigitating reticulum cell and human M cells
-
-
in erythrocytes, gastric cells, renal proximal tubule cells and osteoclasts
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
cathepsin E specifically induces growth arrest and apoptosis in a variety of human prostate cancer cell lines in vitro by catalyzing the proteolytic release of soluble tumor necrosis factor-related apoptosis-inducing ligand from tumor cell surface and prevents tumor growth and metastasis in vivo through multiple mechanisms, including induction of apoptosis angiogenesis inhibition and enhanced immune responses
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATE_HUMAN
396
0
42794
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
42000
76000
82000
90000
additional information
additional information
-
amino acid composition and sequence of procathepsin E from rabbit, guinea pig and human
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
the native enzyme is a dimer that can yield 2 catalytically active subunit molecules of MW 40000-45000 upon exposition to mild reducing conditions
additional information
-
native cathepsin E is a dimer consisting of 2 identical catalytically active subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
enzymes: N-glycosylated with high-mannose type oligosaccharide chain
glycoprotein
-
human and rat erythrocyte enzyme: endo-beta-N-acetylglucosaminidase H-resistant complex or hybrid-type oligosaccharide chain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion, crystal structure of an activation intermediate of cathepsin E at 2.35 A resolution. The overall structure follows the general fold of aspartic proteases of the A1 family, and the intermediate shares many features with the intermediate 2 on the proposed activation pathway of aspartic proteases like pepsin C and cathepsin D. The pro-sequence is cleaved from the protease and remains stably associated with the mature enzyme by forming the outermost sixth strand of the interdomain beta-sheet
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
-
75% loss of activity of erythrocyte membrane aspartic proteinase from human erythrocytes, inactivation of slow-moving proteinase from human gastric mucosa and cathepsin E from rat spleen, instable above pH 5.8
30780
additional information
additional information
-
the pH-stability of the mutant monomeric form in alkaline solution is markedly reduced
30802
additional information
-
resists inactivation upon sequential exposure to acid and alkaline conditions
30782
additional information
-
monomeric cathepsin E is much less stable in weakly alkaline solution than dimeric form
30798
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
additional information
55
-
20 min, inactivation of native enzyme at pH 5.5, only 10% loss of recombinant enzyme activity
55
-
t1/2: 35 min (native enzyme) or 1.7 min (recombinant enzyme) at pH 7.5, t1/2: less than 5 min at pH 8.5
additional information
-
no difference in thermostability between recombinant and native enzyme forms
additional information
-
the temperature stability of the mutant monomeric form in alkaline solution is markedly reduced
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP, CTP or GTP stabilizes in the range of pH 5-7.4, not below pH 5, adenosine, sodium triphosphate, ADP, 2,3-diphosphoglycerate do not stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
as procathepsin E with following activation by lowering the pH-value of the solution to 4
-
recombinant from heterologous Chinese hamster ovary cells (3 forms: cytosolic s-CE and vacuolar v-CE-1 and 2)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
HEK-293 cells are transfected with the full length human cathepsin E gene cloned into pcDNA3.1V5His
-
human pro-cathepsin E is expressed in Escherichia coli in the form of inclusion bodies. The protein is dissolved in 8 M guanidinium chloride and refolded by dilution/dialysis. The main side products in the refolding reaction were soluble, high molecular mass protein complexes linked most likely due to formation of wrong intra- and intermolecular disulfide bonds. Pro-cathepsin E auto-activates at pH 3.5. The major part of the high molecular mass complexes is easily removed during the auto-activation process as these protein components precipitate during the pH shifts
-
stable expression in human prostate carcinoma cell line ALVA101, product is named ALVA101/hCE
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cathepsin E mRNA is highly upregulated in a human pancreatic ductal adenocarcinoma and pancreatic intraepithelial neoplasia lesions as well as in genetically engineered mouse models of pancreatic cancer
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
-
CatE is essential for processing of ovalbumin by murine B-cells, Cat E could play a major role in antigen processing, involvement of CatE in the MHC class II pathway
medicine
-
combination of cathepsin E and doxorubicin is sufficient to overcome resistance to tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in chemoresistant prostate cancer PPC-1 cells
medicine
-
pancreas-bearing pancreatic intraepithelial neoplasia lesions and pancreatic tumours show an elevated expression of cathepsin E, allowing selective in-vivo detection of human pancreatic ductal adenocarcinoma xenografts and imaging of pancreas with pancreatic intraepithelial neoplasia lesions and pancreatic tumours in genetically engineered mouse models of pancreatic cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamamoto, K.; Ueno, E.; Uemura, H.; Kato, Y.
Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E
Biochem. Biophys. Res. Commun.
148
267-272
1987
Homo sapiens, Rattus norvegicus
Jupp, R.A.; Richards, A.D.; Kay, J.; Dunn, B.M.; Wyckoff, J.B.; Samloff, M.; Yamamoto, K.
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E
Biochem. J.
254
895-898
1988
Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
Azuma, T.; Pals, G.; Mohandas, T.K.; Couvreur, J.M.; Taggert, R.T.
Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases
J. Biol. Chem.
264
16748-16753
1989
Homo sapiens
Ueno, E.; Sakai, H.; Kato, Y.; Yamamoto, K.
Activation mechanism of erythrocyte cathepsin E. evidence for the occurrence of the membrane-associated active enzyme
J. Biochem.
105
878-882
1989
Homo sapiens
Thomas, D.J.; Richards, A.D.; Jupp, R.A.; Ueno, E.; Yamamoto, K.; Samloff, I.M.; Dunn, B.M.; Kay, J.
Stabilisation of cathepsin E by ATP
FEBS Lett.
243
145-148
1989
Homo sapiens
Athauda, S.B.P.; Matsuzaki, O.; Kageyama, T.; Takahashi, K.
Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E
Biochem. Biophys. Res. Commun.
168
878-885
1990
Homo sapiens
Athauda, S.B.P.; Takahashi, T.; Inoue, H.; Ichinose, M.; Takahashi, K.
Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin
FEBS Lett.
292
53-56
1991
Homo sapiens
Athauda, S.B.P.; Takahashi, T.; Kageyama, T.; Takahashi, K.
Autocatalytic processing of procathepsin E to cathepsin E and their structural differences
Biochem. Biophys. Res. Commun.
175
152-158
1991
Homo sapiens
Robinson, P.S.; Lees, W.E.; Kay, J.; Cook, N.D.
Kinetic parameters for the generation of endothelins-1,-2 and -3 by human cathepsin E
Biochem. J.
284
407-409
1992
Homo sapiens
Kiselev, A.F.; Gul'nik, S.V.; Tarasova, N.I.
Human stomach cathepsin E action on human immunoglobulins
Adv. Exp. Med. Biol.
306
369-371
1991
Homo sapiens
Takeda-Ezaki, M.; Yamamoto, K.
Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes
Arch. Biochem. Biophys.
304
352-358
1993
Homo sapiens
Athauda, S.B.P.; Arakawa, H.; Nishigai, M.; Takahashi, T.; Takahashi, K.
Inhibition of cathepsin E by alpha 2-macroglobulin and the resulting structural changes in the inhibitor
J. Biochem.
113
526-530
1993
Homo sapiens
Tsukuba, T.; Hori, H.; Azuma, T.; Takahashi, T.; Taggart, R.T.; Akamine, A.; Ezaki, M.; Nakanishi, H.; Sakai, H.; Yamamoto, K.
Isolation and characterization of recombinant human cathepsin E expressed in Chinese hamster ovary cells
J. Biol. Chem.
268
7276-7282
1993
Homo sapiens
Hill, J.; Montgomery, D.S.; Kay, J.
Human cathepsin E produced in E. coli
FEBS Lett.
326
101-104
1993
Homo sapiens
Kageyama, T.
Procathepsin E and cathepsin E
Methods Enzymol.
248
120-136
1995
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Iida, H.; Matsuba, T.; Yamada, M.; Azuma, T.; Suzuki, H.; Yamamoto, K.; Hori, H.
Purification and characterization of recombinant human cathepsin E
Adv. Exp. Med. Biol.
362
325-330
1995
Homo sapiens
Athauda, S.B.P.; Kageyama, T.; Takahashi, T.; Inoue, H.; Ichinose, M.; Ukai, M.; Takahashi, K.
Isolation and characterization of human gastric procathepsin E and cathepsin E
Adv. Exp. Med. Biol.
362
201-210
1995
Homo sapiens
Tsukuba, T.; Masayuki, Y.; Hori, H.; Azuma, T.; Yamamoto, K.
Comparison of biochemical properties of natural and recombinant cathepsin E
Adv. Exp. Med. Biol.
362
331-334
1995
Homo sapiens
Fowler, S.D.; Kay, J.; Dunn, B.M.; Tatnell, P.J.
Monomeric human cathepsin E
FEBS Lett.
366
72-74
1995
Homo sapiens
Kageyama, T.; Takahashi, K.
A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization
J. Biochem.
87
725-735
1980
Homo sapiens
Arnold, D.; Keilholz, W.; Schild, H.; Dumrese, T.; Stevanovic, S.; Rammensee, H.G.
Substrate specificity of cathepsins D and E determined by N-terminal and C-terminal sequencing of peptide pools
Eur. J. Biochem.
249
171-179
1997
Homo sapiens
Athauda, S.B.; Takahashi, K.
Distinct cleavage specificity of human cathepsin E at neutral pH with special preference for Arg-Arg bonds
Protein Pept. Lett.
9
15-22
2002
Homo sapiens
Chou, K.C.
Modeling the tertiary structure of human cathepsin-E
Biochem. Biophys. Res. Commun.
331
56-60
2005
Homo sapiens
Yasuda, Y.; Kohmura, K.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
A new selective substrate for cathepsin E based on the cleavage site sequence of alpha2-macroglobulin
Biol. Chem.
386
299-305
2005
Homo sapiens, Rattus norvegicus
Chain, B.M.; Free, P.; Medd, P.; Swetman, C.; Tabor, A.B.; Terrazzini, N.
The expression and function of cathepsin E in dendritic cells
J. Immunol.
174
1791-1800
2005
Homo sapiens, Mus musculus
Ostermann, N.; Gerhartz, B.; Worpenberg, S.; Trappe, J.; Eder, J.
Crystal structure of an activation intermediate of cathepsin E
J. Mol. Biol.
342
889-899
2004
Homo sapiens
Cappiello, M.G.; Wu, Z.; Scott, B.B.; McGeehan, G.M.; Harrison, R.K.
Purification and characterization of recombinant human cathepsin E expressed in human kidney cell line 293
Protein Expr. Purif.
37
53-60
2004
Homo sapiens
Page, J.L.; Strom, S.C.; Omiecinski, C.J.
Regulation of the human cathepsin E gene by the constitutive androstane receptor
Arch. Biochem. Biophys.
467
132-138
2007
Homo sapiens
Zaidi, N.; Kalbacher, H.
Cathepsin E: a mini review
Biochem. Biophys. Res. Commun.
367
517-522
2008
Homo sapiens, Mus musculus
Shin, M.; Kadowaki, T.; Iwata, J.; Kawakubo, T.; Yamaguchi, N.; Takii, R.; Tsukuba, T.; Yamamoto, K.
Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
Biol. Chem.
388
1173-1181
2007
Homo sapiens
Zaidi, N.; Herrmann, T.; Baechle, D.; Schleicher, S.; Gogel, J.; Driessen, C.; Voelter, W.; Kalbacher, H.
A new approach for distinguishing cathepsin E and D activity in antigen-processing organelles
FEBS J.
274
3138-3149
2007
Homo sapiens
Burster, T.; Reich, M.; Zaidi, N.; Voelter, W.; Boehm, B.O.; Kalbacher, H.
Cathepsin E regulates the presentation of tetanus toxin C-fragment in PMA activated primary human B cells
Biochem. Biophys. Res. Commun.
377
1299-1303
2008
Homo sapiens (P14091), Homo sapiens
Caruso, M.; Moore, J.; Goodall, G.J.; Thomas, M.; Phillis, S.; Tyskin, A.; Cheetham, G.; Lerda, N.; Takahashi, H.; Ruszkiewicz, A.
Over-expression of cathepsin E and trefoil factor 1 in sessile serrated adenomas of the colorectum identified by gene expression analysis
Virchows Arch.
454
291-302
2009
Homo sapiens (P14091)
Yasukochi, A.; Kawakubo, T.; Nakamura, S.; Yamamoto, K.
Cathepsin E enhances anticancer activity of doxorubicin on human prostate cancer cells showing resistance to TRAIL-mediated apoptosis
Biol. Chem.
391
947-958
2010
Homo sapiens
Kwan, J.C.; Eksioglu, E.A.; Liu, C.; Paul, V.J.; Luesch, H.
Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation
J. Med. Chem.
52
5732-5747
2009
Homo sapiens
Abd-Elgaliel, W.R.; Tung, C.H.
Selective detection of Cathepsin E proteolytic activity
Biochim. Biophys. Acta
1800
1002-1008
2010
Homo sapiens
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