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Information on EC 3.4.23.34 - cathepsin E and Organism(s) Rattus norvegicus and UniProt Accession P16228
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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: Rattus norvegicus
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
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
-
-
-
-
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
MOCAc-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(DnP)-D-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2 + H2O
?
-
fluorogenic synthetic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Ile-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 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Ser-Ala-Phe-Leu-Ala-Phe-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
?
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
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(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
-
-
?
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
-
i.e. RS-6
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
CCACCAACACAACTAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 4.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAACAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 31.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAACGAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 14.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAATAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCATCACTACAACAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCATAGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 22.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCATAGTGCTCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 6.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCCCACCACAACCCTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 37.6% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCCCACCACAACCCTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
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)-Nle-Arg-Leu
-
i.e. H-297, 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
TCCATAAGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGAATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 26.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGATTCACTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGCTCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 24.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGTCACTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 18.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGTATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 15.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGAGCTCACTCATCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 27.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGAGCTCACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGTGCTCACTTATCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 19.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TGCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 40.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TTCATATGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TTCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 29.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IGCEERSFPNIIIIIG
-
up to 260% activation of cythepsin E, KD value about 300 nM. Treatment of HeLa cells with cathepsin E and peptide results in decrease in cell viability, with a 1.5- and 3-fold increase in the level of apoptosis in comparison to cells treated with cathepsin E alone
additional information
-
screening for cathepsin E-activity-enhancing peptides functioning in the physiological pH range as potential cancer therapeutic candidates
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.27 - 1.91
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
0.0032
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
0.0028
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
0.00153 - 0.00228
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
0.00243
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Ser-Ala-Phe-Leu-Ala-Phe-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
additional information
additional information
-
pH-dependence of kinetic constants
-
1.27
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, wild-type
1.31
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant D98E
1.91
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant T284S
0.00153
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
0.00179
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
0.00228
(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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.55 - 11.9
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
39.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
32.2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
1.68
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Ser-Ala-Phe-Leu-Ala-Phe-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
additional information
additional information
-
pH-dependence of kinetic constants
-
1.55
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant D98E
6.4
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant T284S
11.9
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, wild-type
0.52
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
13.58
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
18.8
(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
20.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000112
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
-
0.0000165
Ascaris pepsin inhibitor
-
40°C, pH 4.0, gastric cathepsin E, hydrolysis of (7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
0.0000056
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
0.0000078
pepstatin A
-
40°C, pH 4.0, gastric 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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_RAT
398
0
43021
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
-
2 * 51000, monomer CE-I, gel filtration, treated with 2-mercaptoethanol
additional information
additional information
-
amino acid composition and sequence of procathepsin E from rabbit, guinea pig and human
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 51000, monomer CE-I, gel filtration, treated with 2-mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
propeptide of cathepsin E is essential for the correct folding, maturation, and targeting of this protein to its final destination
glycoprotein
-
enzymes: N-glycosylated with high-mannose type oligosaccharide chain
glycoprotein
-
N-glycosylation of cathepsin E plays an important role in its processing, maturation and trafficking to the appropriate destination in the cells, but is not necessarily essential for its correct folding
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D98A/D283A
N324D
-
N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation
N92Q
-
N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation
N92Q/N374D
-
N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation
additional information
-
construction of two fusion proteins using chimeric DNAs encoding the cathepsin E propeptide fused to the mature cathepsin D tagged with HA at the COOH terminus and encoding the cathepsin D propeptide fused to the mature cathepsin E
D98A/D283A
-
mutant enzyme has no catalytic activity on either protein or synthetic substrates. In contrast with wild-type cathepsin E, the mutant enzyme is neither processed nor matured even after a 24-h chase period, but stably remains as a 46000 Da precursor
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
-
monomeric cathepsin E is much less stable in weakly alkaline solution than dimeric form
30798
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of two fusion proteins using chimeric DNAs encoding the cathepsin E propeptide fused to the mature cathepsin D tagged with HA at the COOH terminus and encoding the cathepsin D propeptide fused to the mature cathepsin E
-
mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells
-
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
Yonezawa, S.; Fujii, K.; Maejima, Y.; Tamoto, K.; Mori, Y.; Muto, N.
Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form
Arch. Biochem. Biophys.
267
176-183
1988
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
Wiederanders, B.; Schaper, S.; Kirschke, H.
Isolation and some properties of a cathepsin E type proteinase from rat spleen
Biomed. Biochim. Acta
48
23-32
1989
Rattus norvegicus
Yonezawa, S.; Takahashi, T.; Ichinose, M.; Miki, K.; Tanaka, J.; Gasa, S.
Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme
Biochem. Biophys. Res. Commun.
166
1032-1038
1990
Rattus norvegicus
Kageyama, T.
Procathepsin E and cathepsin E
Methods Enzymol.
248
120-136
1995
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Okamoto, K.; Yu, H.; Misumi, Y.; Ikehara, Y.; Yamamoto, K.
Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E
Arch. Biochem. Biophys.
322
103-111
1995
Rattus norvegicus
Liu, J.; Tsukuba, T.; Okamoto, K.; Ohishi, M.; Yamamoto, K.
Mutational analysis of residues in two consensus motifs in the active sites of cathepsin E
J. Biochem.
132
493-499
2002
Rattus norvegicus
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
Tsukuba, T.; Ikeda, S.; Okamoto, K.; Yasuda, Y.; Sakai, E.; Kadowaki, T.; Sakai, H.; Yamamoto, K.
Characterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells
FEBS J.
273
219-229
2006
Rattus norvegicus
Yasuda, Y.; Tsukuba, T.; Okamoto, K.; Kadowaki, T.; Yamamoto, K.
The role of the cathepsin E propeptide in correct folding, maturation and sorting to the endosome
J. Biochem.
138
621-630
2005
Rattus norvegicus
Kitamura, K.; Yoshida, C.; Kinoshita, Y.; Kadowaki, T.; Takahashi, Y.; Tayama, T.; Kawakubo, T.; Naimuddin, M.; Salimullah, M.; Nemoto, N.; Hanada, K.; Husimi, Y.; Yamamoto, K.; Nishigaki, K.
Development of systemic in vitro evolution and its application to generation of peptide-aptamer-based inhibitors of cathepsin E
J. Mol. Biol.
387
1186-1198
2009
Rattus norvegicus (P16228)
Yoshida, C.; Kuniwake, A.; Naimuddin, M.; Nishigaki, K.
Molecular design guided by a local map of sequence space: DNA aptamers that inhibit cathepsin E
Oligonucleotides
18
1-8
2008
Rattus norvegicus
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