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Information on EC 3.4.24.15 - thimet oligopeptidase and Organism(s) Rattus norvegicus and UniProt Accession P24155

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.15 thimet oligopeptidase
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This record set is specific for:
Rattus norvegicus
UNIPROT: P24155 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues
Synonyms
metallopeptidase, ep24.15, thimet oligopeptidase, pz-peptidase, endopeptidase 24.15, ep 24.15, thop1, endo-oligopeptidase a, endo-oligopeptidase, endooligopeptidase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bradykinin-inactivating endopeptidase
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EC 3.4.99.31
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endo-oligopeptidase A
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endopeptidase 24.15
endopeptidase EC 3.4.24.15
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metalloendopeptidase 24.15
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metalloendopeptidase EC 3.4.24.15
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metallopeptidase
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MP78
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neutral endopeptidase 24.15
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peptidase, thimet oligo-
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Pz-peptidase
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soluble metallo-endopeptidase
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soluble metallopeptidase
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thimet peptidase
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thiol-dependent metalloendopeptidase
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additional information
CAS REGISTRY NUMBER
COMMENTARY hide
110639-28-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
a fluorescent-quenched substrate
-
-
?
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin + H2O
?
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl + H2O
?
show the reaction diagram
-
-
?
Abz-GFDPFRQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
?
alpha-neoendorphin + H2O
?
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin-(1-7) + ?
show the reaction diagram
-
-
-
?
beta-neoendorphin + H2O
?
show the reaction diagram
-
-
-
?
dynorphin 1-8 + H2O
?
show the reaction diagram
-
-
-
?
gondotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-OH
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile + Arg-Arg-Ala-Lys-dinitrophenyl
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu + Arg-Arg-Ala-Lys-dinitrophenyl
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH + H2O
?
show the reaction diagram
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
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-
?
(7-methoxycoumarin-4-yl)actayl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-AFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-AF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-AKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-DFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-DF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-EFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-EF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-ENKPRRPYIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(ortho-aminobenzoyl)-ENKPR + RPYIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (ortho-aminobenzoyl)-KPRRP + YIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
84% cleavage at R-R bond, 16% cleavage at P-Y bond
-
?
(o-aminobenzoyl)-ENKPRRPYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPR + RPYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
16% cleavage at P-Y bond, 40% cleavage at Y-Q bond, 44% cleavage at R-R
-
?
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-FFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GASP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GDSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GESP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFAP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFDP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFEP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFFP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFHP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFIP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFLP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFNP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFPP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFQP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFRP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSA + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSD + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSE + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSF + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSL + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSN + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + ARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + DRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + ERQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FQQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
72% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRA-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRE-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRF-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRI-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRL-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRN-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRP-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRR-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRS-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPFRSSRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSPFRS + SRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
14% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
8% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + HRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + IRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + LRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + NRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + QRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSQ + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSR + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSS + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GHSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GISP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GLSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GNSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GPSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GQSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GRSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GSSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-HFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-IFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-IF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-KPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-LF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LYENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-LYENKPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LYENKPRRP + YILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (ortho-aminobenzoyl)-LYENKPRRPY + ILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
68% cleavage at P-Y bond, 32% cleavage at Y-I bond
-
?
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NAPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-NF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKAR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKPRRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKPR + RAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
(o-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-Phe-Arg-Lys-(dinitrophenyl-proline) + H2O
(o-aminobenzoyl)-Phe-Arg + Lys-(dinitrophenyl-proline)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-QFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-QF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
(o-aminobenzoyl)-RPPGFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
23% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-SFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-SF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-GGFLRRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
2-aminobenzoyl-GGFL + RRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + 2-aminobenzoyl-GGFLR + RDQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
absence of Ca2+, 37% cleavage of R-R bond and 63% cleavage of L-R bond. Presence of 50 mM Ca2+, 74% cleavage of R-R bond and 26% of L-R bond
-
-
?
2-aminobenzoyl-GGFLRRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
2-aminobenzoyl-GGFL + RRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + 2-aminobenzoyl-GGFLR + RVQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
absence of Ca2+, 64% cleavage of R-R bond and 36% cleavage of L-R bond. Presence of 50 mM Ca2+, 79% cleavage of R-R bond and 21% of L-R bond
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
show the reaction diagram
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-PLGPdK-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol + H2O
?
show the reaction diagram
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
-
?
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin + H2O
?
show the reaction diagram
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
-
?
7-methoxycoumaryl-4-acetyl-Pro-Leu-Gly-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
?
7-methoxycoumaryl-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
?
7-methoxycoumatin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
-
-
?
Abz-GFSAFRQ-EDDnp + H2O
Abz-GFSA + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSEFRQ-EDDnp + H2O
Abz-GFSE + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSFFRQ-EDDnp + H2O
Abz-GFSF + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSHFRQ-EDDnp + H2O
Abz-GFSH + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSI + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSLFRQ-EDDnp + H2O
Abz-GFSL + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSQFRQ-EDDnp + H2O
Abz-GFSQ + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSRFRQ-EDDnp + H2O
Abz-GFSR + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSSFRQ-EDDnp + H2O
Abz-GFSS + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSWFRQ-EDDnp + H2O
Abz-GFSW + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSYFRQ-EDDnp + H2O
Abz-GFSY + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
adrenorphin
peptide fragments
show the reaction diagram
-
-
-
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
show the reaction diagram
-
i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11
-
-
?
angiotensin I + H2O
?
show the reaction diagram
-
33.5% of the activity with bradykinin
-
?
angiotensin II + H2O
?
show the reaction diagram
-
7% of the activity with bradykinin
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
show the reaction diagram
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
show the reaction diagram
-
i.e. angiotensin II, cleavage site: Tyr4-Ile5
-
?
benzoyl-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Arg + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
benzoyl-Asp-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Asp + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly + H2O
benzoyl-Gly + Ala-Ala-Gly
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate + H2O
benzoyl-Gly-Arg + Ala-Ala-Phe-4-aminobenzoate
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate + H2O
benzoyl-Gly-Asp + Ala-Ala-Phe-4-aminobenzoate
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Lys-Arg + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-Ala-Phe-p-aminobenzoate
show the reaction diagram
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
-
-
?
cholecystokinin-8
peptide fragments
show the reaction diagram
-
sulfated
-
-
?
corticotropin-like intermediate lobe peptide
peptide fragments
show the reaction diagram
-
-
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
show the reaction diagram
-
-
-
?
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from peptidylprolyl isomerase A
-
-
?
GFGDLKSPAGLQV + H2O
GFGDLK + SPAGLQV
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation elongation factor 1beta2
-
-
?
IHSLPPEGKLG
IHSLPPE + GKLG
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from cytochrome c oxidase subunit VIII
-
-
?
KDIEDVFYKY
KDIEDVF + YKY
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from arginine/serine-rich splicing factor 1
-
-
?
luliberin
peptide fragments
show the reaction diagram
-
-
-
-
?
LVVYPWTQRY + H2O
?
show the reaction diagram
-
0.72% of the activity with bradykinin, cleavage sites: LVVYP-/-W-/-T-/-Q-/-RY
-
?
Met-enkephalin-Arg6-Gly7-Leu8
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Arg-N-(2,4-dinitrophenyl)ethylenediamine
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Val-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
show the reaction diagram
-
-
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
show the reaction diagram
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg + Arg-Pro-Tyr-Ile-Leu
show the reaction diagram
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
show the reaction diagram
-
-
-
-
?
PVNFKFLSH + H2O
?
show the reaction diagram
-
140% of the activity with bradykinin, cleavage sites: PVNF-/-K-/-F-/-LSH
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
show the reaction diagram
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ?
show the reaction diagram
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(1–5). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor
-
?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation initiation factor 5A
-
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
show the reaction diagram
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
show the reaction diagram
-
dynorphin 1-17
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
Tyr-Gly-Gly-Phe-Leu + Arg-Lys-Tyr-Pro
show the reaction diagram
-
beta-neoendorphin
-
?
vasoactive intestinal peptide
peptide fragments
show the reaction diagram
-
-
-
-
?
VVYPWTQRY + H2O
?
show the reaction diagram
-
10.6% of the activity with bradykinin, cleavage sites: VVYPW-/-T-/-Q-/-RY
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-neoendorphin + H2O
?
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin-(1-7) + ?
show the reaction diagram
-
-
-
?
beta-neoendorphin + H2O
?
show the reaction diagram
-
-
-
?
dynorphin 1-8 + H2O
?
show the reaction diagram
-
-
-
?
gondotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
?
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from peptidylprolyl isomerase A
-
-
?
GFGDLKSPAGLQV + H2O
GFGDLK + SPAGLQV
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation elongation factor 1beta2
-
-
?
IHSLPPEGKLG
IHSLPPE + GKLG
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from cytochrome c oxidase subunit VIII
-
-
?
KDIEDVFYKY
KDIEDVF + YKY
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from arginine/serine-rich splicing factor 1
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
show the reaction diagram
-
gonadotropin-releasing hormone, the enzyme degrades gonadotropin-releasing hormone, GnRH, by cleaving the central Tyr5-Gly6 bond
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ?
show the reaction diagram
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(1–5). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor
-
?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
show the reaction diagram
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation initiation factor 5A
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
increases the affinity for the substrate 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitropheyol
Ca2+
-
extracellular Ca2+ concentration has no effect on the total amount of extracellular enzyme. Absence of Ca2+ favors the enzyme shedding from the plasma membrane into the medium. In presence of Ca2+, change of preference to R-R bonds instead of L-R bonds of substrates 2-aminobenzoyl-GGFLRRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) and 2-aminobenzoyl-GGFLRRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Co2+
-
restores activity after EDTA treatment
additional information
-
metallopeptidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
JA-2
specific inhibition
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Aib-Tyr-4-aminobenzoate
specific TOP enzyme inhibitor JA-2
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Aib-Tyr-p-aminobenzoate
specific inhibitor JA-2
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
(3-aminopropanoyl)-Pro-Pro-Gly-Phe-(3-aminopropanoic acid)-Pro-Phe-Arg
-
no degradation by EC 3.4.24.15
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
1,10-phenanthroline
-
-
angiotensin I
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
angiotensin II
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
Arg-Pro-Ala-Gly-Phe-(3-aminopropanoyl)-Pro-Phe-Arg
-
no degradation by EC 3.4.24.15
Arg-Pro-Pro-Ala-Phe-(3-aminopropanoyl)-Pro-Phe-Arg
-
low degradation by EC 3.4.24.15
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
IC50: 0.007 mM, degradation by EC 3.4.24.15
ATP
-
Zn2+ at the active center of the enzyme is the target for the ATP binding to the enzyme leading to the peptidase inhibition and to the enzyme autophosphorylation
bradykinin
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
captopril
-
0.005 mM
dithiothreitol
dynorphin A1-13
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
HVVR-4-nitroanilide
-
-
JA-2
-
i.e. N-[1-(R,S)-carboxy-3-phenylpropyl]Ala-Aib-Tyrp-aminobenzoate, the aromatic ring of Tyr605 was an important anchor for its interaction with wild-type TOP
leupeptin
-
weak
LVVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
N-(1-(R,S)-carboxy-3-phenylpropyl)-L-Ala-L-Ala-L-Tyr-p-aminobenzoate
-
-
N-(1-(RS)-carboxy-3-phenylpropyl)-Ala-Aib-Tyr-p-aminobenzoate
-
-
N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate
-
0.005 mM
N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
the inhibitor is degraded at the Ala-Tyr bond, thus severely limiting its utility in vivo
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Phe-(3-aminopropanoic acid)
-
IC50: 0.0063 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)
-
IC50: 0.0069 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3R)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)
-
IC50: 0.0794 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3S)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)
-
IC50: 0.0631 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-(2-aminomethyl-3-phenylpropionyl)-(3-aminopropanoic acid)
-
IC50: 0.158 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Phe-(3-aminopropanoic acid)
-
IC50: 0.0028 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Tyr-3-aminopropanoic acid
-
IC50: 0.0063 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-aminopropanoyl)-Tyr-(3-aminopropanoic acid)
-
IC50: 0.0056 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(alpha-aminoisobutyryl)-Tyr-p-aminobenzoate
-
the inhibitor remains stable after 48 h with all tissues examined. The inhibitor inhibits the closely related endopeptidase EC 3.4.24.15 1/20 to 1/30 as potently as it inhibits EC 3.4.24.15
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Phe-(3-aminopropanoic acid)
-
IC50: 0.01 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)
-
IC50: 0.0056 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-((3S)-3-amino-4-(4-hydroxyphenyl)butanoyl)-(3-aminopropanoic acid)
-
IC50: 0.0251 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-beta-2-Phe-(3-aminopropanoylic acid)
-
IC50: 0.04 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-(3-aminopropanoic acid)
-
IC50: 0.0036 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-pAB
-
i.e. cFP-AAF-pAB, a transition state analogue inhibitor specific for EP24.15
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-(3-aminopropanoic acid)
-
IC50: 0.00012 mM, complete degradation by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
IC50: 0.00006 mM, potent and specific inhibitor, unstable in vivo due to cleavage between the alanine and tyrosine residues by the enzyme nephrilysin. This cleavage generates a potent inhibitor of angiotensin converting enzyme, thereby limiting the use of the inhibitor for in vivo studies
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-(3-aminopropanoic acid)
-
IC50: 0.00079 mM, no cleavage by nephrilysin
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Tyr-(3-aminopropanoic acid)
-
IC50: 0.00066 mM, no cleavage by nephrilysin
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate
-
-
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
-
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-p-aminobenzoate
-
-
p-hydroxymercuribenzoate
-
-
PVNFKFLSH
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
RPPG-((3R)-3-amino-4-phenylbutanoic acid)-SPFR
RPPG-((3S)-3-amino-4-phenylbutanoic acid)-SPFR
RPPG-(2-aminomethyl-3-phenylpropionic acid)-SPFR
-
no degradation by EC 3.4.24.15
RPPGF-((3R)-3-amino-4-hydroxybutanoic acid)-PFR
-
no degradation by EC 3.4.24.15
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
i.e. dynorphin-(1-13)
VVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
Zn2+
-
above 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cocaine
cocaine treatment causes an increase in the ventral striatum in enzyme specific activity and enzyme relative mRNA amount determined by real time RT-PCR
H2O2
synergistic effect of antimycin A, succinate, and antimycin A plus succinate on activation by H2O2. Antimycin A and succinate stimulate the H2O2 production and increase rTOP activity
2-mercaptoethanol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of 2-mercaptoethanol
dithiothreitol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of dithiothreitol
GSSG
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, maximal activity by partial S-glutathionylation, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000057 - 0.00127
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
0.004 - 0.01
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
-
0.014 - 0.037
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
0.0025
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0014
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0012 - 0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
0.0045
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0102
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.003
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.001
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0042
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0166
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0225
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00071
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0068
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0052
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00072
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00099
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00038
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00027
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0149
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0053
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0076
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.004
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.037
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.018
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.002
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0139
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.119
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0019
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0126
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0044
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.131
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0203
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0048
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0005
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00057
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0059
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
0.0022
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00019
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.007
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0085
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.005
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0073
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0075
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0022
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0048
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0028
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0099
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0036
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00016
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00082
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0071
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00078
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.064
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.036
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.015
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0124
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0015
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.021
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0028
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.114
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.007
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0121
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0015 - 0.0043
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.023 - 0.0343
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
0.00401 - 0.009
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
0.000041 - 0.0021
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
0.0012 - 0.0098
Abz-GFSAFRQEDDnp
0.0021 - 0.0075
Abz-GFSEFRQEDDnp
0.0007 - 0.016
Abz-GFSFFRQEDDnp
0.0076 - 0.0096
Abz-GFSHFRQEDDnp
0.0004 - 0.005
Abz-GFSIFRQEDDnp
0.0016 - 0.0102
Abz-GFSLFRQEDDnp
0.0012 - 0.0058
Abz-GFSQFRQEDDnp
0.0011 - 0.01
Abz-GFSRFRQEDDnp
0.0037 - 0.02
Abz-GFSSFRQEDDnp
0.0008 - 0.0074
Abz-GFSWFRQEDDnp
0.0009 - 0.011
Abz-GFSyFRQEDDnp
0.067
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
3.1 - 3.45
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
1.54 - 2.5
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
0.058 - 0.83
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
0.37
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate
-
-
-
0.72
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate
-
-
-
1.36 - 2
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
0.24
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
0.16
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.39 - 0.51
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
0.031
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.012 - 0.0161
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
0.095
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
-
0.037
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
0.1 - 0.22
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
0.06
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile
-
-
0.038
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 1.07
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
0.027 - 9.9
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
0.025 - 11.2
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
0.00052 - 1.26
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
2.6 - 9.8
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.75
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1 - 4.7
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.53 - 6.08
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.6
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
2.5
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.2
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.8
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.7
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.4
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
4
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.3
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.89 - 6.08
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
4.9
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.5
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.6
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.8
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.7
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
10.2
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
24.7
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.7
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.7
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.4
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.9
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
18.5
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
8.2 - 8.9
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.5 - 1.8
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
2.3
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
4
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.6 - 11.8
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.1
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.8 - 3
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
11.1
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
3.1
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
4.2 - 7.9
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
7
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.82 - 6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
17.5
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.1
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.1
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
4.8
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
12.3
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.6
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.77 - 6.08
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
4.3
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.2 - 1.4
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
5.3
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
3.8 - 5.9
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.74 - 6.08
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
10.1
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
12.3
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
2.7
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
21.5
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.5
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.8
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
14.5
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.4
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
11.5
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.2
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
11.5
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.9
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
13.3
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.2
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.94 - 6.08
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
2.2 - 3.8
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
3.6
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.75 - 3
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
8
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
4.2
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
8.7
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
5.7
(o-aminobenzoyl)-NKPRRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
-
1.1 - 4.7
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
4.3
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.67 - 6.08
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
3.2
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.3
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.7
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1.4 - 6.3
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.00037 - 2.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
0.1 - 1.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
2.6 - 10.4
Abz-GFSAFRQEDDnp
1.5 - 5.3
Abz-GFSEFRQEDDnp
6.7 - 27.3
Abz-GFSFFRQEDDnp
1.8 - 24.7
Abz-GFSHFRQEDDnp
0.001 - 13.6
Abz-GFSIFRQEDDnp
3.4 - 13.6
Abz-GFSLFRQEDDnp
5.8 - 12.1
Abz-GFSQFRQEDDnp
0.6 - 7
Abz-GFSRFRQEDDnp
1.5 - 8.8
Abz-GFSSFRQEDDnp
0.2 - 9.1
Abz-GFSWFRQEDDnp
6.2 - 20.4
Abz-GFSyFRQEDDnp
33.8
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
5.3
benzoyl-Gly-Ala-Ala-Gly
-
-
1.15
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
3.1 - 17
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
4.77 - 179
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
5.25
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate
-
-
-
2.2
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate
-
-
-
1.45 - 4.54
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
10.1
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
2.75 - 8.6
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
19.2
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
6.2
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
12
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
-
7.9
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
21.5 - 94.1
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
86.4
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile
-
-
37.9
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000142 - 0.0000298
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
0.0004
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.014
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.25
ADP
-
-
0.00429
angiotensin I
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00812
angiotensin II
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.042
ATP
-
-
0.00536
bradykinin
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00004
dynorphin A1-13
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00256
LVVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.000023
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(alpha-aminoisobutyryl)-Tyr-p-aminobenzoate
-
-
0.02776
PVNFKFLSH
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.01002
VVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Rattus norvegicus
-
IC50: 0.007 mM, degradation by EC 3.4.24.15
0.0063
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Phe-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0063 mM, no cleavage by nephrilysin
0.0069
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0069 mM, no cleavage by nephrilysin
0.0794
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3R)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0794 mM, no cleavage by nephrilysin
0.0631
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3S)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0631 mM, no cleavage by nephrilysin
0.158
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-(2-aminomethyl-3-phenylpropionyl)-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.158 mM, no cleavage by nephrilysin
0.0028
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Phe-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0028 mM, no cleavage by nephrilysin
0.0063
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Tyr-3-aminopropanoic acid
Rattus norvegicus
-
IC50: 0.0063 mM, no cleavage by nephrilysin
0.0056
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-aminopropanoyl)-Tyr-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0056 mM, no cleavage by nephrilysin
0.01
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Phe-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.01 mM, no cleavage by nephrilysin
0.0056
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0056 mM, no cleavage by nephrilysin
0.0251
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-((3S)-3-amino-4-(4-hydroxyphenyl)butanoyl)-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0251 mM, no cleavage by nephrilysin
0.04
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-beta-2-Phe-(3-aminopropanoylic acid)
Rattus norvegicus
-
IC50: 0.04 mM, no cleavage by nephrilysin
0.0036
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.0036 mM, no cleavage by nephrilysin
0.00012
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.00012 mM, complete degradation by nephrilysin
0.00006
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
Rattus norvegicus
-
IC50: 0.00006 mM, potent and specific inhibitor, unstable in vivo due to cleavage between the alanine and tyrosine residues by the enzyme nephrilysin. This cleavage generates a potent inhibitor of angiotensin converting enzyme, thereby limiting the use of
0.00079
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.00079 mM, no cleavage by nephrilysin
0.00066
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Tyr-(3-aminopropanoic acid)
Rattus norvegicus
-
IC50: 0.00066 mM, no cleavage by nephrilysin
0.012
RPPG-((3R)-3-amino-4-phenylbutanoic acid)-SPFR
Rattus norvegicus
-
IC50: 0.012 mM
0.02
RPPG-((3S)-3-amino-4-phenylbutanoic acid)-SPFR
Rattus norvegicus
-
IC50: 0.02 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
assay at
8.2
-
above
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
pH 7.0: about 45% of maximal activity, pH 9.5: about 40% of maximal activity
additional information
-
pH-dependence of wild-type and mutant enzymes, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
hypophysial portal blood
Manually annotated by BRENDA team
-
cultured trigeminal ganglia, similar expression profile of enzyme and type 2 bradykinin receptor
Manually annotated by BRENDA team
additional information
-
presence of EP24.15 in the perivascular space of the median eminence and secretion into portal blood
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space
Manually annotated by BRENDA team
additional information
-
EP24.15 does not contain a membrane anchoring motif yet it is localised to the extracellular surface of the plasma membrane
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
malfunction
-
inhibition of EP24.15 activity with a specific inhibitor augments the steroid-induced luteinizing hormone increase in ovariectomized rats
metabolism
-
EP24.15 is the main enzyme of luteinizing hormone-releasing hormone, i.e. LHRH, metabolism as the prime mediator of LHRH-I degradation in both the brain and periphery
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THOP1_RAT
687
0
78385
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000 - 70000
-
gel filtration
70000
-
1 * 70000, SDS-PAGE
72985
-
x * 72985, calculation from nucleotide sequence
78000
-
x * 78000, SDS-PAGE
78300
-
x * 78300, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
active form, stabilized by H2O2
dimer
-
in vitro oligomerization upon S-glutathionylation of the cysteinyl-rich enzyme, the oligomerization has a regulatory function, overview
monomer
trimer
-
in vitro oligomerization upon S-glutathionylation of the cysteinyl-rich enzyme, the oligomerization has a regulatory function, overview
additional information
-
Ala607 of TOP contributes to the flexibility of the loops formed by residues 599-611, i.e. GHLAGGYDAQYYG, in TOP, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
the enzyme activity is dependent upon phosphorylation by protein kinase A on serine residue 644. Phosphorylation of this conserved site reduces enzyme affinity for binding LHRH-I
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C246S/C248S/C253S
site-directed mutagenesis, the mutations abolish the DTT and H2O2 effects on rTOP activity. The triple-mutated rTOP is not affected by DTT
Y612F
the ratio of turnover-number to Km-value is 0.2% of the wild-type ratio. The Ki-value for N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate is 2fold higher than the wild-type value
A607G
-
site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
D159A
-
similar to wild-type regarding enzymatic activity, secondary structure, calcium sensitivity and immunoreactivity
D93A
-
similar to wild-type regarding enzymatic activity, secondary structure, calcium sensitivity and immunoreactivity. Reduced ability to associate with the plasma membrane
D93A/D153A
-
similar to wild-type regarding enzymatic activity, secondary structure, calcium sensitivity and immunoreactivity. Reduced ability to associate with the plasma membrane
E502A
-
complete loss of enzymatic activity
G599A
-
decrease in the activity towards the 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH substrates, with little effect or in activity towards 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
G603A
-
increase in preference for the five-residue 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol substrate and, to a lesser extent, for the 10-residue 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH substrate
G603A/G604A
-
increase in preference for the five-residue 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol substrate and, to a lesser extent, for the 10-residue 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH substrate
G603P
-
decrease in catalytic activity towards all substrates tested
G604A
-
decrease in the activity towards the 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH substrates, with little effect or in activity towards 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
G611A
-
decrease in the activity towards the 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH substrates, with little effect or in activity towards 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
H473A
-
complete loss of enzymatic activity
H474A
-
complete loss of enzymatic activity
H477A
-
complete loss of enzymatic activity
Y605A
-
site-directed mutagenesis, the mutation does not affect the overall fold of the protein, TOP Y605A is inhibited less efficiently by JA-2, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
Y605F
Y605F/Y612F
-
marked decrease in catalytic activity, but neither Y605 nor Y612 is necessary for hydrolysis of 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
Y612F
-
marked decrease in catalytic activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
unstable above
37063
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
H2O2 stabilizes the monomeric enzyme form
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
H2O2 activates the enzyme
753583
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by glutathione affinity chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis by quantitative real-time PCR
gene Thop1, recombinant expression of wild-type and mutant enzymes
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
large-scale expression in Escherichia coli
-
recombinant enzyme from testis, expression in HEK-293 cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cocaine treatment causes an increase in the ventral striatum in enzyme specific activity and enzyme relative mRNA amount determined by real time RT-PCR
expression and activity of thimet oligopeptidase are increased in the hippocampus of in rats during the acute phase of pilocarpine-induced epilepsy model
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
thermal unfolding is a two-step process with a major endotherm at a Tm of 64°C and a minor endotherm at a Tm of 55°C
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dahms, P.; Mentlein, R.
Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16
Eur. J. Biochem.
208
145-154
1992
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
McKie, N.; Dando, P.M.; Brown, M.A.; Barrett, A.J.
Rat thimet oligopeptidase: large-scale expression in Escherichia coli and characterization of the recombinant enzyme
Biochem. J.
309
203-207
1995
Rattus norvegicus
Manually annotated by BRENDA team
Tisljar, U.; Barrett, A.J.
Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit
Biochem. J.
267
531-533
1990
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Orlowski, M.; Reznik, S.; Ayala, J.; Pierotti, A.R.
Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides
Biochem. J.
261
951-958
1989
Rattus norvegicus
Manually annotated by BRENDA team
Barrett, A.J.; Brown, M.A.; Dando, P.M.; Knight, C.G.; McKie, N.; Rawlings, N.D.; Serizawa, A.
Thimet oligopeptidase and oligopeptidase M or neurolysin
Methods Enzymol.
248
529-556
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Pierotti, A.; Dong, K.W.; Glucksman, M.J.; Orlowski, M.; Roberts, J.L.
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15 [published erratum appears in Biochemistry 1994 Jan 18;33(2):622]
Biochemistry
29
10323-10329
1990
Rattus norvegicus
Manually annotated by BRENDA team
Orlowski, M.; Michaud, C.; Chu, T.G.
A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
Eur. J. Biochem.
135
81-88
1983
Rattus norvegicus
Manually annotated by BRENDA team
Oliveira, V.; Campos, M.; Hemerly, J.P.; Ferro, E.S.; Camargo, A.C.; Juliano, M.A.; Juliano, L.
Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4.24.16): comparison with thimet oligopeptidase (EC 3.4.24.15) and neprilysin (EC 3.4.24.11)
Anal. Biochem.
292
257-265
2001
Rattus norvegicus
Manually annotated by BRENDA team
Shrimpton, C.N.; Abbenante, G.; Lew, R.A.; Smith, A.I.
Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15
Biochem. J.
345
351-356
2000
Rattus norvegicus
-
Manually annotated by BRENDA team
Oliveira, V.; Campos, M.; Melo, R.L.; Ferro, E.S.; Camargo, A.C.; Juliano, M.A.; Juliano, L.
Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
Biochemistry
40
4417-4425
2001
Rattus norvegicus
Manually annotated by BRENDA team
Steer, D.; Lew, R.; Perlmutter, P.; Smith, A.I.; Aguilar, M.I.
Inhibitors of metalloendopeptidase EC 3.4.24.15 and EC 3.4.24.16 stabilized against proteolysis by the incorporation of beta-amino acids
Biochemistry
41
10819-10826
2002
Rattus norvegicus
Manually annotated by BRENDA team
Portaro, F.C.; Hayashi, M.A.; Silva, C.L.; de Camargo, A.C.
Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage
Eur. J. Biochem.
268
887-894
2001
Rattus norvegicus
Manually annotated by BRENDA team
Lew, R.A.; Boulos, E.; Stewart, K.M.; Perlmutter, P.; Harte, M.F.; Bond, S.; Reeve, S.B.; Norman, M.U.; Lew, M.J.; Aguilar, M.I.; Smith, I.
Substrate analogues incorporating b-amino acids: potential application for peptidase inhibition
FASEB J.
15
1664-1666
2001
Rattus norvegicus
Manually annotated by BRENDA team
Sigman, J.A.; Edwards, S.R.; Pabon, A.; Glucksman, M.J.; Wolfson, A.J.
pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)
FEBS Lett.
545
224-228
2003
Rattus norvegicus (P24155)
Manually annotated by BRENDA team
Rioli, V.; Gozzo, F.C.; Heimann, A.S.; Linardi, A.; Krieger, J.E.; Shida, C.S.; Almeida, P.C.; Hyslop, S.; Eberlin, M.N.; Ferro, E.S.
Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
J. Biol. Chem.
278
8547-8555
2003
Rattus norvegicus
Manually annotated by BRENDA team
Molina, H.M.; Carmona, A.K.; Kouyoumdjian, M.; Borges, D.R.
Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase
Life Sci.
67
509-520
2000
Rattus norvegicus
Manually annotated by BRENDA team
Sigman, J.A.; Patwa, T.H.; Tablante, A.V.; Joseph, C.D.; Glucksman, M.J.; Wolfson, A.J.
Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies
Biochem. J.
388
255-261
2005
Rattus norvegicus (P24155)
Manually annotated by BRENDA team
Oliveira, V.; Garrido, P.A.; Rodrigues, C.C.; Colquhoun, A.; Castro, L.M.; Almeida, P.C.; Shida, C.S.; Juliano, M.A.; Juliano, L.; Camargo, A.C.; Hyslop, S.; Roberts, J.L.; Grum-Tokars, V.; Glucksman, M.J.; Ferro, E.S.
Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity
FEBS J.
272
2978-2992
2005
Rattus norvegicus
Manually annotated by BRENDA team
Saric, T.; Graef, C.I.; Goldberg, A.L.
Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases
J. Biol. Chem.
279
46723-46732
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Jeske, N.A.; Berg, K.A.; Cousins, J.C.; Ferro, E.S.; Clarke, W.P.; Glucksman, M.J.; Roberts, J.L.
Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia
J. Neurochem.
97
13-21
2006
Rattus norvegicus
Manually annotated by BRENDA team
Ahmed, M.M.; Arif, M.; Chikuma, T.; Kato, T.
Pentylenetetrazol-induced seizures affect the levels of prolyl oligopeptidase, thimet oligopeptidase and glial proteins in rat brain regions, and attenuation by MK-801 pretreatment
Neurochem. Int.
47
248-259
2005
Rattus norvegicus
Manually annotated by BRENDA team
Machado, M.F.; Rioli, V.; Dalio, F.M.; Castro, L.M.; Juliano, M.A.; Tersariol, I.L.; Ferro, E.S.; Juliano, L.; Oliveira, V.
The role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor binding
Biochem. J.
404
279-288
2007
Rattus norvegicus
Manually annotated by BRENDA team
Demasi, M.; Piassa Filho, G.M.; Castro, L.M.; Ferreira, J.C.; Rioli, V.; Ferro, E.S.
Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation
Free Radic. Biol. Med.
44
1180-1190
2008
Rattus norvegicus
Manually annotated by BRENDA team
Bruce, L.A.; Sigman, J.A.; Randall, D.; Rodriguez, S.; Song, M.M.; Dai, Y.; Elmore, D.E.; Pabon, A.; Glucksman, M.J.; Wolfson, A.J.
Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selection
FEBS J.
275
5607-5617
2008
Rattus norvegicus
Manually annotated by BRENDA team
Berti, D.A.; Morano, C.; Russo, L.C.; Castro, L.M.; Cunha, F.M.; Zhang, X.; Sironi, J.; Klitzke, C.F.; Ferro, E.S.; Fricker, L.D.
Analysis of intracellular substrates and products of thimet oligopeptidase (EC 3.4.24.15) in human embryonic kidney 293 cells
J. Biol. Chem.
284
14105-14116
2009
Rattus norvegicus
Manually annotated by BRENDA team
Wu, T.J.; Pierotti, A.R.; Jakubowski, M.; Sheward, W.J.; Glucksman, M.J.; Smith, A.I.; King, J.C.; Fink, G.; Roberts, J.L.
Endopeptidase EC 3.4.24.15 presence in the rat median eminence and hypophysial portal blood and its modulation of the luteinizing hormone surge
J. Neuroendocrinol.
9
813-822
1997
Rattus norvegicus
Manually annotated by BRENDA team
Cleverly, K.; Wu, T.J.
Is the metalloendopeptidase EC 3.4.24.15 (EP24.15), the enzyme that cleaves luteinizing hormone-releasing hormone (LHRH), an activating enzyme?
Reproduction
139
319-330
2010
Rattus norvegicus
Manually annotated by BRENDA team
Dalio, F.M.; Visniauskas, B.; Bicocchi, E.S.; Perry, J.C.; Freua, R.; Gesteira, T.F.; Nader, H.B.; Machado, M.F.; Tufik, S.; Ferro, E.S.; Andersen, M.L.; Toledo, C.A.; Chagas, J.R.; Oliveira, V.
Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain
Biochem. Biophys. Res. Commun.
419
724-727
2012
Rattus norvegicus (P24155), Rattus norvegicus Wistar (P24155)
Manually annotated by BRENDA team
Simoes, P.S.; Visniauskas, B.; Perosa, S.R.; Yacubian, E.M.; Centeno, R.; Canzian, M.; Lopes-Cendes, I.; Maurer Morelli, C.V.; Carrete, H.; Cavalheiro, E.A.; Tufik, S.; Chagas, J.R.; Mazzacoratti, M.d.a..G.
Expression and activity of thimet oligopeptidase (TOP) are modified in the hippocampus of subjects with temporal lobe epilepsy (TLE)
Epilepsia
55
754-762
2014
Rattus norvegicus (P24155), Homo sapiens (P52888), Homo sapiens
Manually annotated by BRENDA team
Pereira, M.G.; Souza, L.L.; Becari, C.; Duarte, D.A.; Camacho, F.R.; Oliveira, J.A.; Gomes, M.D.; Oliveira, E.B.; Salgado, M.C.; Garcia-Cairasco, N.; Costa-Neto, C.M.
Angiotensin II-independent angiotensin-(1-7) formation in rat hippocampus: involvement of thimet oligopeptidase
Hypertension
62
879-885
2013
Rattus norvegicus (P24155), Rattus norvegicus Wistar (P24155)
Manually annotated by BRENDA team
Icimoto, M.Y.; Ferreira, J.C.; Yokomizo, C.H.; Bim, L.V.; Marem, A.; Gilio, J.M.; Oliveira, V.; Nantes, I.L.
Redox modulation of thimet oligopeptidase activity by hydrogen peroxide
FEBS Open Bio
7
1037-1050
2017
Rattus norvegicus (P24155), Homo sapiens (P52888), Homo sapiens
Manually annotated by BRENDA team