3.4.23.34: cathepsin E
This is an abbreviated version!
For detailed information about cathepsin E, go to the full flat file.
Word Map on EC 3.4.23.34
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3.4.23.34
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cathepsins
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proteinases
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pepstatin
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pepsinogen
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procathepsin
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molecular biology
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gastricsin
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medicine
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foveolar
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non-lysosomal
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3.4.23.5
- 3.4.23.34
- cathepsins
- proteinases
- pepstatin
- pepsinogen
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procathepsin
- molecular biology
- gastricsin
- medicine
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foveolar
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non-lysosomal
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3.4.23.5
Reaction
similar to cathepsin D, but slightly broader specificity =
Synonyms
CatE, Cathepsin D-like acid proteinase, cathepsin D-like aspartic proteinase, cathepsin D-like protease, Cathepsin D-type proteinase, cathepsin E, Cathepsin E-like acid proteinase, CE, CTSE, EMAP, erythrocyte membrane acid proteinase, Erythrocyte membrane aspartic proteinase, gastric mucosa non-pepsin acid proteinase, More, Non-pepsin proteinase, slow moving proteinase, Slow-moving proteinase, SMP
ECTree
3.4.23.34 cathepsin EAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.23.34 - cathepsin E
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
alpha2-Macroglobulin
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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
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CCACCAACACAACTAAACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 4.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCACCACCACAACAAAACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 31.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCACCACCACAACGAAACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 14.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCACCACCACAATAAAACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCATCACTACAACAAAACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCCATAGGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 22.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCCATAGTGCTCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 6.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCCCCACCACAACCCTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 37.6% inhibition (2 nM inhibitor /2 nM cathepsin E)
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CCCCCACCACAACCCTCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
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grassystatin A
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potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin B
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potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin C
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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
TCCATAAGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATAGGAATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 26.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATAGGGATTCACTCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATAGGGCTCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 24.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATAGGGTCACTCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 18.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATAGGTATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCATCGGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 15.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCCCGGAGCTCACTCATCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 27.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCCCGGAGCTCACTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TCCCCGGTGCTCACTTATCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 19.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TGCATCGGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 40.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TTCATATGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
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TTCATCGGGATCACTCCCTCCAC
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inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 29.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
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(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
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i.e. H-77, with reduced isostere as replacement of the-CO-NH- of the peptide bond
(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
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i.e. H-77, 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
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N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
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i.e. L-363,564, hemoglobin as substrate
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
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N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
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N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
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i.e. H-261, with reduced isostere as replacement of the -CO-NH- of the peptide bond
N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
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i.e. H-261, with reduced isostere as replacement of the -CO-NH- of the peptide bond
pepstatin
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as substrate, incubation at pH 7.4 restores; at pH 3 and 5.5, not at pH 7.4
pepstatin
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as substrate, incubation at pH 7.4 restores; at pH 3 and 5.5, not at pH 7.4; oxidized insulin B-chain
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
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i.e. H-297, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
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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
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i.e. H-256, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Phe-Arg-Glu
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i.e. H-256, with reduced isostere as replacement of the -CO-NH- of the peptide bond
additional information
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iodoaceteic acid, EDTA, phosphoramidon on proteolysis of membrane proteins; no (or little) inhibition
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additional information
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1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4); inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
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additional information
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1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4); inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
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additional information
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the computed three-dimensional structure of cathepsin-E and the relevant findings might provide useful insights for designing inhibitors with the desired selectivity
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