Information on EC 3.4.24.15 - thimet oligopeptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.4.24.15
-
RECOMMENDED NAME
GeneOntology No.
thimet oligopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues
show the reaction diagram
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SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EC 3.4.99.31
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endo-oligopeptidase A
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endopeptidase 24.15
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metalloendopeptidase 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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TOP
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CAS REGISTRY NUMBER
COMMENTARY
110639-28-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus licheniformis N22
N22
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-
Manually annotated by BRENDA team
Pz peptidase A and B
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Manually annotated by BRENDA team
Geobacillus sp.
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UniProt
Manually annotated by BRENDA team
Geobacillus sp.
strain MO-1
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Manually annotated by BRENDA team
C57BL/6 mice
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Manually annotated by BRENDA team
female C57BL?6J
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Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
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Manually annotated by BRENDA team
Mus musculus C57BL/6J
female C57BL?6J
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Manually annotated by BRENDA team
strain PAO1 PA-14, gene PA4498
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Manually annotated by BRENDA team
recombinat enzyme
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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inhibition of EP24.15 activity with a specific inhibitor augments the steroid-induced luteinizing hormone increase in ovariectomized rats
malfunction
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suppression of TOP by RNAi results in much less recognition of K562-A3 cells by anti-ELFSYLIEK CTL indicating an involvement of TOP in the endogenous generation of ELFYSLIEK (CTL epitope)
metabolism
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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
metabolism
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thimet oligopeptidase is a metallo-oligopeptidase that participates in the intracellular metabolism of peptides
metabolism
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TOP is regulated by estradiol in female mice
metabolism
Mus musculus C57BL/6J
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TOP is regulated by estradiol in female mice
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physiological function
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EP24.15 can modulate the concentrations of gonadotropin-releasing hormone within the hypothalamo-hypophysial portal blood and thereby plays a physiological role in reproduction
physiological function
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EP24.15 is a soluble, neuropeptide-degrading metalloenzyme and plays a role in the degradation of neuropeptides acting at the external cell surface and in the physiological metabolism of neuropeptides
physiological function
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involvement of EP24.15 in the modulation of hypothalamic luteinizing hormone-releasing hormone, LHRH, neuronal function
physiological function
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many roles of EP24.15 in the metabolism of neuropeptides and in cell regulation, overview
physiological function
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TOP is a neuropeptidase involved in the regulation of several physiological functions including reproduction. Among its substrates is gonadotrophin-releasing hormone, an important hypothalamic hormone that regulates the synthesis and release of estradiol and facilitates female sexual behaviour
physiological function
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Nardilysin and TOP are required, either together or alone, for the generation of a tumor-specific CTL epitope from PRAME, an immunodominant CTL epitope from Epstein-Barr virus protein EBNA3C, and a clinically important epitope from the melanoma protein MART-1. TOP functions as C-terminal trimming peptidase in antigen processing, and nardilysin contributes to both the C-terminal and N-terminal generation of CTL epitopes
physiological function
Mus musculus C57BL/6J
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TOP is a neuropeptidase involved in the regulation of several physiological functions including reproduction. Among its substrates is gonadotrophin-releasing hormone, an important hypothalamic hormone that regulates the synthesis and release of estradiol and facilitates female sexual behaviour
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SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
Geobacillus sp.
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?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
-
fluorogenic substrate
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?
(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
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-
-
?
(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
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-
-
?
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH + H2O
?
show the reaction diagram
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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
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?
(Gly-Pro-Leu)n
Gly-Pro-Leu
show the reaction diagram
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n = 2, 3, 4 and 5, the peptides are cleaved only at Leu-Gly bonds, activity is most rapid with n = 3 and slowest with n = 5. The cleavage fitts a sequential first-order model
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?
(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
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-
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?
(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
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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
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?
(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)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + REQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + FQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + HQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + IQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + LQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + NQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RV-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + YQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
cleavage at the R-R or at the R-X bond
-
?
(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)-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)-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
-
33% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FR-(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)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
85% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(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
-
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-GFSHFRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-GFSH + FRQ-N-(2,4-dinitrophenyl)ethylenediamine
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
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis N22
-
i.e. Pz-peptide
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
4-phenylazobenzyloxycarbonyl-Pro + Leu-Gly-Pro-D-Arg
show the reaction diagram
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg + H2O
?
show the reaction diagram
Geobacillus sp.
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
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(2,4-dinitrophenyl) + H2O
?
show the reaction diagram
Geobacillus sp., Geobacillus sp. MO-1
Q4W803
-
-
-
?
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-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin + H2O
?
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-D-Lys-2,4-dinitrophenyl + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
-
?
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-Pro-Leu-Gly-Pro-Lys-dinitrophenyl + H2O
?
show the reaction diagram
P24155
-
-
?
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-GFSAFRQEDDnp + H2O
Abz-GFSAFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSDFRQ-EDDnp + H2O
Abz-GFSD + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSEFRQ-EDDnp + H2O
Abz-GFSE + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSEFRQEDDnp + H2O
Abz-GFSEFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSFFRQ-EDDnp + H2O
Abz-GFSF + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSFFRQEDDnp + H2O
Abz-GFSFFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSHFRQ-EDDnp + H2O
Abz-GFSH + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSHFRQEDDnp + H2O
Abz-GFSHFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSIFR-EDDnp + H2O
Abz-GFSIFR + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSIFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSI + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSLFRQEDDnp + H2O
Abz-GFSLFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPARQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Ala-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPDRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Asp-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPERQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Glu-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFR-EDDnp + H2O
Abz-GFSPFR + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSPFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSPFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Phe-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPHRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + His-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPIRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Ile-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPLRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Leu-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPQRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Gln-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPRRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Arg-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPSRQ-EDDnp + H2O
Abz-Gly-Phe + Ser-Ala + Ser-Arg-Gln-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSQFRQ-EDDnp + H2O
Abz-GFSQ + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSQFRQEDDnp + H2O
Abz-GFSQFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSRFRQ-EDDnp + H2O
Abz-GFSR + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSRFRQEDDnp + H2O
Abz-GFSRFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSSFRQ-EDDnp + H2O
Abz-GFSS + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSSFRQEDDnp + H2O
Abz-GFSSFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSWFRQ-EDDnp + H2O
Abz-GFSW + FRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSWFRQEDDnp + H2O
Abz-GFSWFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSYFRQEDDnp + H2O
Abz-GFSYFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-NKPRRPQEDDnp + H2O
Abz-NKPRRPQ + EDDnp
show the reaction diagram
-
-
-
-
?
Abz-RPPGFSPFRQEDDnp + H2O
Abz-RPPGFSPFRQ + EDDnp
show the reaction diagram
-
-
-
-
?
adrenorphin
peptide fragments
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
-
-
-
aminobenzyl-Ala-Gly-Leu-Ala-nitrobenzylamide
aminobenzyl-Ala-Gly + Leu-Ala-nitrobenzylamide
show the reaction diagram
-
weak
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid precursor protein-derived substrate
peptide fragments
show the reaction diagram
-
spanning the beta-secretase site Ile-Ser-Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser, cleavage occurs predominantly at Lys-Met and Glu-Phe bonds
-
?
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
-
?
angiotensin-I + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin-II + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
show the reaction diagram
-
cleavage sites: Pro4-Gln5, Phe8-Gly9 and Phe7-Phe8
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
show the reaction diagram
-
i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, Phe8-Gly9
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
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
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
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
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
-
?
ASNENMETM + H2O
?
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
-
-
-
?
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-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
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-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-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-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-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-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-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-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-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-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
inactive with benzoyl-Gly-D-Phe-Ala-Ala-Phe-p-aminobenzoate
-
?
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-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
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
degradation, participation of EP24.15 in the metabolism of bradykinin, bradykinin is internalized via the kinin B2 receptor, EP24.15 attenuates maximal kinin2 receptor responsiveness without influencing the potency of bradykinin to stimulate phosphoinositide hydrolysis and intracellular Ca2+ mobilization, overview
-
-
?
Bradykinin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
cholecystokinin-8
peptide fragments
show the reaction diagram
-
sulfated
-
-
?
Collagen + H2O
?
show the reaction diagram
Geobacillus sp.
-
degradation
-
-
?
Collagen + H2O
?
show the reaction diagram
Geobacillus sp.
-
degradation by Pz peptidase A, Pz peptidase A recognizes collagen-specific tripeptide units, Gly-Pro-Xaa, Pz peptidase A shares common reactions with mammalian thimet oligopeptidase and neurolysin, but has extremely low primary sequence identity to these enzymes
-
-
?
Collagen + H2O
?
show the reaction diagram
Geobacillus sp.
-
the enzyme recognizes the specific sequence Gly-Pro-Xaa of in collagen
-
-
?
corticotropin-like intermediate lobe peptide
peptide fragments
show the reaction diagram
-
-
-
-
?
CPI-0004Na + H2O
?
show the reaction diagram
-
tetrapeptidic prodrug of doxorubicin
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
show the reaction diagram
-
-
-
?
dynorphin A1-8 + 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
-
-
-
ELFSYLIEKVKR + H2O
ELFSYLIEK + VKR
show the reaction diagram
-
purified TOP efficiently cleaves the nardilysin-dependent 12- and 13-residue precursors PRA(190-201) (ELFSYLIEKVKR) and PRA(190-202) (ELFSYLIEKVKRK) directly after the epitope's C-terminal Lys198
-
-
?
ELFSYLIEKVKRK + H2O
ELFSYLIEK + VKRK
show the reaction diagram
-
purified TOP efficiently cleaves the nardilysin-dependent 12- and 13-residue precursors PRA(190-201) (ELFSYLIEKVKR) and PRA(190-202) (ELFSYLIEKVKRK) directly after the epitopes C-terminal Lys198
-
-
?
FAPGNYPAL + H2O
?
show the reaction diagram
-
-
-
?
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
-
-
?
gonadotrophin-releasing hormone + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6J
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin-releasing hormone + H2O
peptide fragments
show the reaction diagram
-
-
-
?
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
-
-
-
LTLRTKL + H2O
LTLR + Thr + Lys-Leu
show the reaction diagram
-
at 91% of the rate with RPPGF-SP-FR
-
-
?
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
-
?
major histocompatibility complex class I-presented antigenic peptides + H2O
?
show the reaction diagram
-
by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
-
?
N-acetyl-Ala-Ala-Ala
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
?
N-succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
degradation
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
i.e. H-Lys-Ile-Pro-Tyr-Ile-Leu-OH
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
-
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
degradation
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
cleavage of Arg-Arg bonds
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
cleavage of the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
determination of specific cleavage sites, overview
-
-
?
neurotensin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
cleavage of Arg-Arg bonds
-
-
?
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-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
-
i.e. luteinizing hormone-releasing hormone
-
-
?
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
-
i.e. luteinizing hormone-releasing hormone
-
?
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
-
i.e. luteinizing hormone-releasing hormone
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
i.e. neurotensin
-
-
?
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
-
i.e. neurotensin
-
-
?
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
-
i.e. neurotensin
-
?
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
-
i.e. neurotensin
-
?
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
-
i.e. neurotensin
-
-
?
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
show the reaction diagram
-
-
-
-
?
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
show the reaction diagram
-
-
-
-
?
propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met
propionyl-Gly-Ser-Pro-(farnesyl-Cys) + Val-Leu-Met
show the reaction diagram
-
-
-
?
pTLRTKL + H2O
phospho-Thr-Leu-Arg + L-tyrosine + Lys-Leu
show the reaction diagram
-
at 10% of the rate with RPPGF-SP-FR
-
-
?
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
-
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.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
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 that cleaves the hormone at the fifth and sixth bond of the decapeptide (Tyr5-Gly6) to form LHRH-(15)
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
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-(15). 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
-
?
RGPGRAFVTI + H2O
?
show the reaction diagram
-
-
-
?
RPPGFSPFR + H2O
RPPGF + Ser-Pro + Phe-Arg
show the reaction diagram
-
-
-
-
?
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
-
-
-
SIINFEKL + H2O
?
show the reaction diagram
-
-
-
?
somatostatin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide
succinyl-Ala-Ala + Ala-4-nitroanilide
show the reaction diagram
-
weak
-
?
succinyl-Ala-Ala-Phe-4-nitroanilide
succinyl-Ala-Ala + Phe-4-nitroanilide
show the reaction diagram
-
weak
-
?
succinyl-Ala-Ala-Val-4-nitroanilide
succinyl-Ala-Ala + Val-4-nitroanilide
show the reaction diagram
-
weak
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
show the reaction diagram
-
-
-
?
TPHPARIGL + H2O
?
show the reaction diagram
-
-
-
?
TYQRTRALV + H2O
?
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 + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
show the reaction diagram
-
i.e. dynorphin A(1-8)
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
show the reaction diagram
-
i.e. dynorphin A(1-8)
-
?
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
-
?
Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
?
show the reaction diagram
-
i.e. angiotensin I
-
-
?
vasoactive intestinal peptide
peptide fragments
show the reaction diagram
-
-
-
-
?
VVYPW-TQ-RY-KL + H2O
VVYPW + Thr-Gln + Arg-Tyr + Lys-Leu
show the reaction diagram
-
at 9% of the rate with RPPGF-SP-FR
-
-
?
VVYPWTQRY + H2O
?
show the reaction diagram
-
10.6% of the activity with bradykinin, cleavage sites: VVYPW-/-T-/-Q-/-RY
-
?
Met-enkephalin-Arg6-Gly7-Leu8
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no activity with Gly-Phe-Leu-Gly-Phe-Ile-Gly-Phe-Leu
-
-
-
additional information
?
-
-
cleaves preferentially bonds on the carboxyl side of hydrophobic amino acids
-
-
-
additional information
?
-
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro
-
-
-
additional information
?
-
-
no hydrolysis of Met-enkephalin
-
-
-
additional information
?
-
-
no cleavage of denatured collagen, hemoglobin and casein
-
-
-
additional information
?
-
-
no hydrolysis of proteins
-
-
-
additional information
?
-
-
no activity with (o-aminobenzoyl)-LGMISLMKRPPGFSPFRSSRI-NH2
-
?
additional information
?
-
-
no activity with (ortho-aminobenzoyl)-PRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine), (ortho-aminobenzoyl)-KPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) or (ortho-aminobenzoyl)-ENKPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
additional information
?
-
-
proposed role in formation of enkephalins
-
-
-
additional information
?
-
-
degradation of the gonadotropin-releasing hormone by the tissue of the hypothalamo-pituitary axis occurs in a two-step mechanism involving both post-proline cleaving enzyme and the metalloendopeptidase 3.4.24.15
-
-
-
additional information
?
-
-
activity in cytosol may be significant for regulation of major histocompatibility complex class I expression. The enzyme form in the extracellular space is significant for neuropeptide processing
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
-
additional information
?
-
-
enzyme modulates intracellular, peptidergic signaling cascades through type 2 bradykinin receptor
-
-
-
additional information
?
-
-
conformational changes due to chemical denaturation are directly correlated with a change in substrate specificity
-
-
-
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues. No substrates: proteasomal degradation peptides of 18-24 residues
-
-
-
additional information
?
-
-
phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values
-
-
-
additional information
?
-
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, overview
-
-
-
additional information
?
-
-
the enzyme cleaves several bioactive peptides at sites similar or different from neurolysin, EC 3.4.24.16
-
-
-
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
-
additional information
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
-
additional information
?
-
-
cleavage sites of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
residues E469, M490, H495, and R498 determine the substrate specificity of thimet oligopeptidase different from closely related neurolysin, EC 3.4.24.16
-
-
-
additional information
?
-
-
substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
-
additional information
?
-
-
the enzyme is involved in the dipeptide transport system, transcriptional Pseudomonas dipeptide regulator PA4499, psdR, negatively regulated the peptidase, PA4498, proteomic profiling of wild-type PAO1 and a PA4499 mutant strains, overview
-
-
-
additional information
?
-
-
identification of intracellular substrates by incubation of HEK-293 cell extract with recombinant enzyme or by overexpression of enzyme in HEK-293 cells. A majority of the potential substrate peptides are 9-11 amino acids in length
-
-
-
additional information
?
-
-
substrate specificity of EP24.15, overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with Abz-GFSLFRQ-EDDnp, Abz-GFSPPRQ-EDDnp, and Abz-GFSPWRQ-EDDnp, overview. Importance of His600 for both substrate binding and/or product release from active site, participation of His600 in TOP catalysis, transferring a proton to the newly generated NH2-terminus or helping Tyr605 and/or Tyr612 in the intermediate oxyanion stabilization
-
-
-
additional information
?
-
Bacillus licheniformis N22
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro, no cleavage of denatured collagen, hemoglobin and casein
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
the enzyme is involved in angiogenesis and tumor growth, overview, substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin-I + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin-II + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
participation of EP24.15 in the metabolism of bradykinin, bradykinin is internalized via the kinin B2 receptor, EP24.15 attenuates maximal kinin2 receptor responsiveness without influencing the potency of bradykinin to stimulate phosphoinositide hydrolysis and intracellular Ca2+ mobilization, overview
-
-
?
Bradykinin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
Geobacillus sp.
-
degradation
-
-
?
Collagen + H2O
?
show the reaction diagram
Geobacillus sp.
-
degradation by Pz peptidase A
-
-
?
dynorphin A1-8 + 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
-
-
?
gonadotrophin-releasing hormone + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6J
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
neuromedin N + H2O
?
show the reaction diagram
-
degradation
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
degradation
-
-
?
neurotensin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
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.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
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-(15). 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
-
-
-
major histocompatibility complex class I-presented antigenic peptides + H2O
?
show the reaction diagram
-
by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
-
?
additional information
?
-
-
proposed role in formation of enkephalins
-
-
-
additional information
?
-
-
degradation of the gonadotropin-releasing hormone by the tissue of the hypothalamo-pituitary axis occurs in a two-step mechanism involving both post-proline cleaving enzyme and the metalloendopeptidase 3.4.24.15
-
-
-
additional information
?
-
-
activity in cytosol may be significant for regulation of major histocompatibility complex class I expression. The enzyme form in the extracellular space is significant for neuropeptide processing
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
-
additional information
?
-
-
enzyme modulates intracellular, peptidergic signaling cascades through type 2 bradykinin receptor
-
-
-
additional information
?
-
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, overview
-
-
-
additional information
?
-
-
the enzyme cleaves several bioactive peptides at sites similar or different from neurolysin, EC 3.4.24.16
-
-
-
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
-
additional information
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the dipeptide transport system, transcriptional Pseudomonas dipeptide regulator PA4499, psdR, negatively regulated the peptidase, PA4498, proteomic profiling of wild-type PAO1 and a PA4499 mutant strains, overview
-
-
-
additional information
?
-
-
identification of intracellular substrates by incubation of HEK-293 cell extract with recombinant enzyme or by overexpression of enzyme in HEK-293 cells. A majority of the potential substrate peptides are 9-11 amino acids in length
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
restores activity after EDTA treatment
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)
Ca2+
-
Ca2+-dependent interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium
Cd2+
-
restores activity after EDTA treatment
Co2+
-
restores activity after EDTA treatment
Co2+
-
restores activity after EDTA treatment
KCl
-
strong activation
Na2SO4
-
strong activation
NaCl
-
strong activation
NaI
-
modest activation
NH4Cl
-
modest activation
Zinc
-
contains about 2 gatoms of zinc per mol of enzyme
Zinc
-
contains 2 gatom of zinc per mol of enzyme, one catalytic zinc and one structural zinc
Zn2+
-
0.001 mM, stimulates
Zn2+
-
most effective ion in restoration of the activity after EDTA treatment
Zn2+
-
restores activity after treatment with EDTA
Zn2+
-
second step of structural unfolding results in complete loss of catalytic Zn2+
Zn2+
-
a zinc-dependent metallopeptidase
Zn2+
-
a zinc-dependent metallopeptidase
Zn2+
-
metalloendopeptidase containing a HEXXHmotif
Zn2+
-
dependent on
Zn2+
-
zinc metalloendopeptidase
Zn2+
-
catalytic zinc, the binding site is rather distinct from the calmodulin/Ca2+ binding site
Zn2+
-
required
Zn2+
-
zinc metalloendopeptidase
Zn2+
-
dependent on
Mn2+
-
restores activity after EDTA treatment
additional information
Geobacillus sp.
-
Pz peptidase A is an intracellular M3 metallopeptidase
additional information
-
metallopeptidase
additional information
-
EP24.15 is a metalloendopeptidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
2-mercaptoethanol
-
-
5-cyano-2-nitrothiobenzoate
-
0.1 mM, 62% inhibition
-
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-Lys-Pro
-
-
Arg-Pro-Pro-Ala-Phe-(3-aminopropanoyl)-Pro-Phe-Arg
-
low degradation by EC 3.4.24.15
Arg-Pro-Pro-Gly-Phe
-
-
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
IC50: 0.007 mM, degradation by EC 3.4.24.15
Arg-Pro-Tyr-Ile-Leu
-
-
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
benzyloxycarbonyl-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Ser
Geobacillus sp.
-
-
bradykinin
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
captopril
-
0.005 mM
Cbz-Phe-PSI[PO2CH2]-Ala-Lys-Ser
Geobacillus sp.
Q4W803
phosphinic peptide inhibitor
-
chymostatin
-
-
Co2+
-
10 mM, complete inhibition
Cu2+
-
10 mM, complete inhibition
Cu2+
-
0.1 mM, 90% inhibition
diethyl dicarbonate
-
reversed by hydroxylamine
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
10 mM, reversible
dynorphin A1-13
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
EDTA
-
-
EDTA
-
-
EDTA
-
no inhibition
EDTA
-
-
EDTA
-
reactivation by metal ions
EDTA
-
reactivation by metal ions
Fe2+
-
-
Fe3+
-
10 mM, complete inhibition
Gly-Pro-Phe-PSI[PO2CH2]-Gly-Pro-Nle
Geobacillus sp.
-
specific for neurolysin
Gly-Pro-Phe-PSI[PO2CH2]-Gly-Pro-Nle
Geobacillus sp.
Q4W803
phosphinic peptide inhibitor
iodoacetate
-
1 mM, 22% inhibition
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
JA-2
-
almost complete inhibition at 0.003 mM
L-phospho-Thr-Leu-Arg-Thr-Lys-Leu
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
Leupeptin
-
weak
LTLRTKL
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
LVVYPW-phenylThr-Gln-Arg-Tyr
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
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-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid
-
-
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-Aib-Tyr-4-aminobenzoate
-
i.e. JA-2, a potent TOP inhibitor
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-Ala-Tyr-p-aminobenzoate
-
-
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
-
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
;
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-p-aminobenzoate
-
-
N-[1-(RS)-carboxyl-2-phenylethyl]-Ala-Ala-Phe-4-amino-benzoate
-
i.e. cFP-AAF-pAB, an active site-directed inhibitor
NEM
-
1 mM, 82% inhibition
NEM
-
-
Ni2+
-
-
o-phenanthroline
-
-
o-phenanthroline
-
complete inhibition at 4 mM
o-phenanthroline
-
strong inhibition
p-hydroxymercuribenzoate
-
-
PCMB
-
0.1 mM, 100% inhibition
PCMB
-
-
phosphoramidon
-
-
Pro-Ile
-
13% inhibition at 1 mM
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
-
IC50: 0.012 mM; no degradation by EC 3.4.24.15
RPPG-((3S)-3-amino-4-phenylbutanoic acid)-SPFR
-
IC50: 0.02 mM; no degradation by EC 3.4.24.15
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
S-nitroso-N-acetylpenicillamine
-
inhibition is prevented by DTT
Ser-Pro-Phe-Arg
-
-
tosyl-Phe-CH3Cl
-
0.1 mM, 15% inactivation
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
i.e. dynorphin-(1-13)
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
i.e. dynorphin-(1-13)
VVYPW-phenylThr-Gln-Arg-Tyr
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
VVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
VVYPWTQRY
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Ser
Geobacillus sp.
-
specific for thimet oligopeptidase
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Tyr
Geobacillus sp.
-
specific for thimet oligopeptidase
Z-Pro-prolinal
-
12% inhibition at 0.001 mM
Zn2+
-
at high concentration
Zn2+
-
10 mM, complete inhibition
Zn2+
-
0.1 mM ZnCl2, complete inhibition
Zn2+
-
above 0.1 mM
LVVYPWTQRY
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
additional information
-
phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values
-
additional information
-
no inhibition by bestatin, captopril, leupeptin, and E64, poor inhibition by PMSF
-
additional information
-
secretion of EP24.15 from AT-t20 cells can be stimulated by A23187 and corticotrophin-releasing hormone and blocked by brefeldin A and nocodazole
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates at low concentrations
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
Calmodulin
-
interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium
Calmodulin/Ca2+
-
Ca2+-dependent interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium
-
dithiothreitol
-
activates at low concentrations
dithiothreitol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of dithiothreitol
thiol
-
stimulation
GSSG
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, maximal activity by partial S-glutathionylation, overview
additional information
-
the mdpA gene is induced in the presence of XPro dipeptides, such as Phe-Pro, Gly-Pro
-
additional information
-
A23187 stimulates secretion of EP24.15, synergistic effects of forskolin with A23187, inhibited by protein kinase A inhibitor KT5720
-
additional information
-
secretion of EP24.15 from AT-t20 cells can be stimulated by A23187 and corticotrophin-releasing hormone and blocked by brefeldin A and nocodazole
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605FY612F, 23C, pH 7.8
0.024
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
wild-type, 23C, pH 7.8
0.034
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y612F, 23C, pH 7.8
0.037
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605F, 23C, pH 7.8
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
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
wild-type, 23C, pH 7.8
0.0025
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G599A, 23C, pH 7.8
0.0026
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G604A, 23C, pH 7.8; mutant Y612F, 23C, pH 7.8
0.0029
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A, 23C, pH 7.8; mutant G603P, 23C, pH 7.8
0.0031
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605FY612F, 23C, pH 7.8
0.0042
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605F, 23C, pH 7.8
0.005
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G611A, 23C, pH 7.8
0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A/G604A, 23C, pH 7.8
0.0045
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.003
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0012
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.001
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0042
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0166
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0225
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00071
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0068
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0052
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0014
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00072
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00099
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00038
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00027
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.006
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0149
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0053
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0012
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0076
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0038
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00069
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0011
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0016
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0016
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.004
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.037
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.018
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.002
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0139
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.119
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0019
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0126
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0017
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0044
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.131
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0203
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0038
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0048
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0012
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00069
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0005
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00057
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0018
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0059
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
0.0022
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00019
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0043
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.007
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0015
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0085
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0045
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.005
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0043
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0018
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0073
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0075
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0022
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0037
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0012
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0005
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0033
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0019
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0007
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0017
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0018
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0007
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0015
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0012
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0023
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0022
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0021
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0006
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C
0.0048
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0028
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0037
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0045
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0037
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0099
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0036
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.006
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0017
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00016
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00082
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.00078
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0015
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0015
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0014
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.0102
(ortho-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.021
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.0028
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.114
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.007
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.0071
(ortho-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.064
(ortho-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.036
(ortho-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.015
(ortho-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.0124
(ortho-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.0121
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.0137
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0015
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0022
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0043
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0123
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-(2,4-ditritrophenyl)Lys
-
-
-
0.0082
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl)
Geobacillus sp.
Q4W803
pH and temperature not specified in the publication
-
0.009
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
-
-
0.023
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
-
-
0.0343
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
-
0.000057
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C
0.00013
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 1.5 M urea
0.00048
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 2.5 M urea
0.00127
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 3.5 M urea
0.00401
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A, 23C, pH 7.8
0.00408
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G599A, 23C, pH 7.8
0.00543
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A/G604A, 23C, pH 7.8
0.00643
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603P, 23C, pH 7.8
0.0067
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G611A, 23C, pH 7.8
0.00788
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
wild-type, 23C, pH 7.8
0.0081
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605FY612F, 23C, pH 7.8
0.0082
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605F, 23C, pH 7.8
0.00825
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G604A, 23C, pH 7.8
0.009
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y612F, 23C, pH 7.8
0.004
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.0, with Ca2+
0.0046
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.8, wild-type enzyme
0.0051
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.8, mutant enzyme Y612F
0.01
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.0, without Ca2+ or at pH 5.8 with or without Ca2+
0.000041
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A/G604A, 23C, pH 7.8
0.000054
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A, 23C, pH 7.8
0.000057
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
wild-type, 23C, pH 7.8
0.00008
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605F, 23C, pH 7.8
0.00009
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G604A, 23C, pH 7.8
0.000129
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G599A, 23C, pH 7.8
0.000136
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G611A, 23C, pH 7.8
0.00051
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605FY612F, 23C, pH 7.8
0.00057
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y612F, 23C, pH 7.8
0.0021
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603P, 23C, pH 7.8
0.0143
Abz-GFSAFRQ-EDDnp
-
pH 7.4, 37C
0.0012
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0047
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0098
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0009
Abz-GFSDFRQ-EDDnp
-
pH 7.4, 37C
0.0011
Abz-GFSEFRQ-EDDnp
-
pH 7.4, 37C
0.0021
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.003
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0075
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0105
Abz-GFSFFRQ-EDDnp
-
pH 7.4, 37C
0.0007
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0033
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.016
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0321
Abz-GFSHFRQ-EDDnp
-
pH 7.4, 37C
0.0076
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0086
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0096
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.112
Abz-GFSIFRQ-EDDnp
-
pH 7.4, 37C
0.0004
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0014
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.005
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0016
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0032
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0102
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0218
Abz-GFSPARQ-EDDnp
-
pH 7.4, 37C
0.0075
Abz-GFSPDRQ-EDDnp
-
pH 7.4, 37C
0.0192
Abz-GFSPERQ-EDDnp
-
pH 7.4, 37C
0.0093
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C
0.0131
Abz-GFSPHRQ-EDDnp
-
pH 7.4, 37C
0.0062
Abz-GFSPIRQ-EDDnp
-
pH 7.4, 37C
0.0122
Abz-GFSPLRQ-EDDnp
-
pH 7.4, 37C
0.0148
Abz-GFSPQRQ-EDDnp
-
pH 7.4, 37C
0.0213
Abz-GFSPRRQ-EDDnp
-
pH 7.4, 37C
0.0135
Abz-GFSPSRQ-EDDnp
-
pH 7.4, 37C
0.0091
Abz-GFSQFRQ-EDDnp
-
pH 7.4, 37C
0.0012
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0054
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0058
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0109
Abz-GFSRFRQ-EDDnp
-
pH 7.4, 37C
0.0011
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0044
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.01
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0127
Abz-GFSSFRQ-EDDnp
-
pH 7.4, 37C
0.0037
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0047
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.02
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0208
Abz-GFSWFRQ-EDDnp
-
pH 7.4, 37C
0.0008
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0015
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.0074
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.0009
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.0023
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
0.011
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.067
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
3.1
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
3.45
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
1.54
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
2.5
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
0.058
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
0.49
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
0.83
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
0.37
benzoyl-Gly-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
0.72
benzoyl-Gly-Asp-Ala-Ala-Phe-p-aminobenzoate
-
-
1.36
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
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
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
0.51
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
0.031
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.38
bradykinin
-
-
0.012
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0133
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0161
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
recombinant enzyme from E. coli
0.0732
Gly-Pro-Leu
-
-
0.048
Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0149
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0135
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0026
neurotensin
-
recombinant wild-type enzyme, pH 7.5, 37C
0.0033
neurotensin
-
recombinant mutant E469R/R498T, pH 7.5, 37C
1.64
neurotensin
-
-
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
-
-
32.5
propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met
-
-
0.1
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
-
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
-
-
0.0154
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
additional information
additional information
-
kinetics of wild-type and mutant TOP
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605FY612F, 23C, pH 7.8
0.061
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y612F, 23C, pH 7.8
1.4
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605F, 23C, pH 7.8
11.2
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
wild-type, 23C, pH 7.8
0.00052
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y612F, 23C, pH 7.8
0.0015
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605FY612F, 23C, pH 7.8
0.00449
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603P, 23C, pH 7.8
0.012
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605F, 23C, pH 7.8
0.11
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G604A, 23C, pH 7.8
0.18
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G599A, 23C, pH 7.8
0.3
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G611A, 23C, pH 7.8
0.33
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
wild-type, 23C, pH 7.8
1.22
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A/G604A, 23C, pH 7.8
1.26
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A, 23C, pH 7.8
2.6
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
9.8
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
1
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
4.7
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
0.53
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.4
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.6
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
2.5
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
2.2
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
5.8
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
5.7
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3.4
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
4
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
5.3
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.89
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.08
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
4.9
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
2.5
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
1.6
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
1.8
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
7.7
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
10.2
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
24.7
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.7
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.7
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
7
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3.4
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
8.9
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
18.5
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
8.2
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
8.9
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.5
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.8
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
2.3
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
4
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.6
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
11.8
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.1
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
1.8
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
3
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
11.1
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
3.1
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
4.2
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
7.9
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
7
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
0.82
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
2.3
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
17.5
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3.1
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
7.1
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
4.8
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
12.3
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
2.6
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C; pH 7.4, 37C, cleavage of P-F bond; pH 7.4, 37C, cleavage of P-X bond
0.77
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.08
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
4.3
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
1.2
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.4
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
5.3
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
3.8
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
5.9
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
0.74
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
4.2
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
10.1
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
12.3
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
2.7
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
21.5
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-X bond
1.5
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.3
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
8.8
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6.3
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3.2
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
1
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
1.1
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.2
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.3
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-F bond
0.6
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-H bond
1.6
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.1
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-I bond
0.7
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.2
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.5
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-L bond
0.3
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-N bond
0.6
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
1.8
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
3.3
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
2
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
1.4
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
0.2
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-Y bond
0.3
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37C, cleavage of the R-R bond
14.5
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
8.4
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
11.5
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
5.2
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
11.5
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
2.9
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
13.3
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
3.2
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
6
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
0.94
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
1.5
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
2.2
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
3.8
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
0.75
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
3
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
1.1
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
4.7
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
4.3
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
0.67
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
4.1
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C, cleavage of F-S bond
0.75
(ortho-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
3.2
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.3
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
3.6
(ortho-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
8
(ortho-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
4.2
(ortho-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
8.7
(ortho-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
5.7
(ortho-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
0.7
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C, hydrolysis of R-R bond
1.4
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
4.7
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
6.3
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.3
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C
0.72
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 1.5 M urea
0.91
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 2.5 M urea
1.07
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23C, presence of 3.5 M urea
0.00037
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y612F, 23C, pH 7.8
0.0023
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605FY612F, 23C, pH 7.8
0.0026
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603P, 23C, pH 7.8
0.0086
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605F, 23C, pH 7.8
0.03
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G599A, 23C, pH 7.8
0.11
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G604A, 23C, pH 7.8
0.193
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G611A, 23C, pH 7.8
0.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
wild-type, 23C, pH 7.8
2.32
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A, 23C, pH 7.8
2.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A/G604A, 23C, pH 7.8
0.027
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.8, mutant enzyme Y612F
9.9
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
pH 7.8, wild-type enzyme
0.1
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605FY612F, 23C, pH 7.8
0.18
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603P, 23C, pH 7.8
0.27
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A/G604A, 23C, pH 7.8
0.28
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A, 23C, pH 7.8
0.3
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
wild-type, 23C, pH 7.8
0.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605F, 23C, pH 7.8
0.53
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G604A, 23C, pH 7.8
0.75
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y612F, 23C, pH 7.8
0.86
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G599A, 23C, pH 7.8
1.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G611A, 23C, pH 7.8
11.1
Abz-GFSAFRQ-EDDnp
-
pH 7.4, 37C
2.6
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
10.2
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
10.4
Abz-GFSAFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
0.3
Abz-GFSDFRQ-EDDnp
-
pH 7.4, 37C
1.6
Abz-GFSEFRQ-EDDnp
-
pH 7.4, 37C
1.5
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
3.2
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
5.3
Abz-GFSEFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
5.9
Abz-GFSFFRQ-EDDnp
-
pH 7.4, 37C
6.7
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
12.7
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
27.3
Abz-GFSFFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
13.3
Abz-GFSHFRQ-EDDnp
-
pH 7.4, 37C
1.8
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
15.1
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
24.7
Abz-GFSHFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
0.19
Abz-GFSIFRQ-EDDnp
-
pH 7.4, 37C
0.001
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
5
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
13.6
Abz-GFSIFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
3.4
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
7
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
13.6
Abz-GFSLFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
1.7
Abz-GFSPARQ-EDDnp
-
pH 7.4, 37C
0.03
Abz-GFSPDRQ-EDDnp
-
pH 7.4, 37C
0.01
Abz-GFSPERQ-EDDnp
-
pH 7.4, 37C
2.9
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C
0.3
Abz-GFSPHRQ-EDDnp
-
pH 7.4, 37C
0.04
Abz-GFSPIRQ-EDDnp
-
pH 7.4, 37C
0.02
Abz-GFSPLRQ-EDDnp
-
pH 7.4, 37C
0.7
Abz-GFSPQRQ-EDDnp
-
pH 7.4, 37C
4.5
Abz-GFSPRRQ-EDDnp
-
pH 7.4, 37C
0.4
Abz-GFSPSRQ-EDDnp
-
pH 7.4, 37C
7
Abz-GFSQFRQ-EDDnp
-
pH 7.4, 37C
5.8
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
6.3
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
12.1
Abz-GFSQFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
9.1
Abz-GFSRFRQ-EDDnp
-
pH 7.4, 37C
0.6
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
1.5
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
7
Abz-GFSRFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
9.2
Abz-GFSSFRQ-EDDnp
-
pH 7.4, 37C
1.5
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
1.7
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
8.8
Abz-GFSSFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
6
Abz-GFSWFRQ-EDDnp
-
pH 7.4, 37C
0.2
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
2.7
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
9.1
Abz-GFSWFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
6.2
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged wild-type enzyme
6.4
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605F
20.4
Abz-GFSyFRQEDDnp
-
pH 7.4, 37C, recombinant GST-tagged mutant Y605A
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
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
17
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
4.77
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
48.3
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
179
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
5.25
benzoyl-Gly-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
2.2
benzoyl-Gly-Asp-Ala-Ala-Phe-p-aminobenzoate
-
-
1.45
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
4.54
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
10.1
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
2.75
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
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
-
-
2.3
neurotensin
-
recombinant wild-type enzyme, pH 7.5, 37C
4.2
neurotensin
-
recombinant mutant E469R/R498T, pH 7.5, 37C
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
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
-
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
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1600
Abz-GFSAFRQ-EDDnp
-
pH 7.4, 37C
40660
333
Abz-GFSDFRQ-EDDnp
-
pH 7.4, 37C
40666
1417
Abz-GFSEFRQ-EDDnp
-
pH 7.4, 37C
40665
561
Abz-GFSFFRQ-EDDnp
-
pH 7.4, 37C
40661
414
Abz-GFSHFRQ-EDDnp
-
pH 7.4, 37C
40668
2
Abz-GFSIFRQ-EDDnp
-
pH 7.4, 37C
27615
78
Abz-GFSPARQ-EDDnp
-
pH 7.4, 37C
40669
8
Abz-GFSPDRQ-EDDnp
-
pH 7.4, 37C
40675
1
Abz-GFSPERQ-EDDnp
-
pH 7.4, 37C
40674
317
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C
8875
20.6
Abz-GFSPHRQ-EDDnp
-
pH 7.4, 37C
40677
10
Abz-GFSPIRQ-EDDnp
-
pH 7.4, 37C
40670
8
Abz-GFSPLRQ-EDDnp
-
pH 7.4, 37C
40671
47
Abz-GFSPQRQ-EDDnp
-
pH 7.4, 37C
40673
211
Abz-GFSPRRQ-EDDnp
-
pH 7.4, 37C
40676
30
Abz-GFSPSRQ-EDDnp
-
pH 7.4, 37C
40672
771
Abz-GFSQFRQ-EDDnp
-
pH 7.4, 37C
40664
839
Abz-GFSRFRQ-EDDnp
-
pH 7.4, 37C
40667
724
Abz-GFSSFRQ-EDDnp
-
pH 7.4, 37C
40663
288
Abz-GFSWFRQ-EDDnp
-
pH 7.4, 37C
40662
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0004
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
0.014
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37C
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)
0.00009
Cbz-Phe-PSI[PO2CH2]-Ala-Lys-Ser
Geobacillus sp.
Q4W803
pH and temperature not specified in the publication
-
0.00004
dynorphin A1-13
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.0000192
Gly-Pro-Phe-PSI[PO2CH2]-Gly-Pro-Nle
Geobacillus sp.
-
recombinant Pz peptidase B
0.000088
Gly-Pro-Phe-PSI[PO2CH2]-Gly-Pro-Nle
Geobacillus sp.
Q4W803
pH and temperature not specified in the publication
0.0000889
Gly-Pro-Phe-PSI[PO2CH2]-Gly-Pro-Nle
Geobacillus sp.
-
recombinant Pz peptidase A
0.0063
L-phospho-Thr-Leu-Arg-Thr-Lys-Leu
-
pH 8.0, 37C
0.0026
LTLRTKL
-
pH 8.0, 37C
0.0008
LVVYPW-phenylThr-Gln-Arg-Tyr
-
pH 8.0, 37C
0.0021
LVVYPWTQRY
-
pH 8.0, 37C
0.000023
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(alpha-aminoisobutyryl)-Tyr-p-aminobenzoate
-
-
0.0000142
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
pH 7.8, wild-type enzyme
0.0000298
N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate
-
pH 7.8, mutant enzyme Y612F
0.02776
PVNFKFLSH
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.0046
VVYPW-phenylThr-Gln-Arg-Tyr
-
pH 8.0, 37C
0.0014
VVYPWTQRY
-
pH 8.0, 37C
0.01002
VVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.0000378
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Ser
Geobacillus sp.
-
recombinant Pz peptidase B
0.0000901
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Ser
Geobacillus sp.
-
recombinant Pz peptidase A
0.000043
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Tyr
Geobacillus sp.
-
recombinant Pz peptidase B
0.0000877
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Tyr
Geobacillus sp.
-
recombinant Pz peptidase A
0.00256
LVVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
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
-
IC50: 0.0063 mM, no cleavage by nephrilysin
0.0056
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-aminopropanoyl)-Tyr-(3-aminopropanoic acid)
-
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)
-
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)
-
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)
-
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)
-
IC50: 0.04 mM, no cleavage by nephrilysin
0.0036
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-(3-aminopropanoic acid)
-
IC50: 0.0036 mM, no cleavage by nephrilysin
0.00012
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-(3-aminopropanoic acid)
-
IC50: 0.00012 mM, complete degradation by nephrilysin
0.00006
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
0.00079
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-(3-aminopropanoic acid)
-
IC50: 0.00079 mM, no cleavage by nephrilysin
0.00066
N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Tyr-(3-aminopropanoic acid)
-
IC50: 0.00066 mM, no cleavage by nephrilysin
0.012
RPPG-((3R)-3-amino-4-phenylbutanoic acid)-SPFR
-
IC50: 0.012 mM
0.02
RPPG-((3S)-3-amino-4-phenylbutanoic acid)-SPFR
-
IC50: 0.02 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00037
-
-
0.1
-
purified recombinant enzyme, substrate peptide GFSPFRQ
19.5
Geobacillus sp.
-
purified recombinant Pz peptidase B
30.4
Geobacillus sp.
-
purified recombinant Pz peptidase A
additional information
-
-
additional information
-
substrate specificity, and cell proliferation assay, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 7.5
-
-
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
-
7.5
-
assay at
7.5
-
assay at
8.2
-
above
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: about 35% of maximal activity, pH 8.5: about 45% of maximal activity
6.5 - 8.5
-
more than 50% of maximal activity at pH 6.5 and at pH 8.5
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
additional information
-
pH-profiles of TOP H600A mutant and wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
aortic endothelial cell culture. Enzyme is sensitive to Gialpha2/3 inhibition. Under cyclic strain conditions, level of secreted enzyme increases 2.6fold
Manually annotated by BRENDA team
-
a pituitary tumour cell line
Manually annotated by BRENDA team
-
melanoma cell line
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
melanoma cell line
-
Manually annotated by BRENDA team
-
hypophysial portal blood
Manually annotated by BRENDA team
-
mainly in central nervous system
Manually annotated by BRENDA team
-
treated with pentylenentetrazol, an antagonist of GABAa receptor ion channel binding site. Significant decrease of enzyme activity and protein in the hippocampus after administration of pentylenentetrazol, pretreatment with MK-801 recovered the change of activity
Manually annotated by BRENDA team
-
median eminence and preoptic area in close proximity with LHRH cell bodies
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
Bacillus licheniformis N22
-
-
-
Manually annotated by BRENDA team
-
aortic endothelial cell culture. Enzyme is sensitive to Gialpha2/3 inhibition. Under cyclic strain conditions, level of secreted enzyme increases 2.6fold
Manually annotated by BRENDA team
-
cultured trigeminal ganglia, similar expression profile of enzyme and type 2 bradykinin receptor
Manually annotated by BRENDA team
-
hypothalamic neuronal cell
Manually annotated by BRENDA team
-
hypothalamic cell line, shows low level secretion of EP24.15
Manually annotated by BRENDA team
-
EP24.15 colocalizes with calmodulin in the cytosol of resting HEK293 cells
Manually annotated by BRENDA team
-
colon cancer cell line
Manually annotated by BRENDA team
-
anterior pituitary
Manually annotated by BRENDA team
-
the nuclear thimet oligopeptidase is coexpressed with estrogen receptor alpha in hypothalamic cells, and also in ventrolateral portion of the ventromedial hypothalamic nucleus and the midbrain central grey
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
the nuclear thimet oligopeptidase is coexpressed with estrogen receptor alpha in hypothalamic cells, and also in ventrolateral portion of the ventromedial hypothalamic nucleus and the midbrain central grey
-
Manually annotated by BRENDA team
-
longitudinal smooth muscle membranes and circular smooth muscle membranes
Manually annotated by BRENDA team
-
embryonic kidney
Manually annotated by BRENDA team
-
neuroblastoma cells
Manually annotated by BRENDA team
-
primary culture
Manually annotated by BRENDA team
-
LHRH neurons
Manually annotated by BRENDA team
-
ileum, longitudinal and circular
Manually annotated by BRENDA team
-
recombinant enzyme
Manually annotated by BRENDA team
-
high enzyme content
Manually annotated by BRENDA team
additional information
-
ubiquitous expression
Manually annotated by BRENDA team
additional information
-
wide distribution
Manually annotated by BRENDA team
additional information
-
during embryonic development, EP24.15 is localized in the same neuroanatomical regions as LHRH and LHRH-(1-5)
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
GeneOntology No.
LITERATURE
SOURCE
-
secretion to the medium
Manually annotated by BRENDA team
-
EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space
Manually annotated by BRENDA team
-
activity in cytosol may be significant for regulation of major histocompatibility complex class I expression
Manually annotated by BRENDA team
-
EP24.15 colocalizes with calmodulin in the cytosol of resting HEK293 cells
Manually annotated by BRENDA team
-
the enzyme form in the extracellular space is significant for neuropeptide processing
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
biotinylated enzyme is released into the cell media similar to constitutive release. Secretion inhibitor glyburide decreases the amount of enzyme released into media
-
Manually annotated by BRENDA team
-
secreted enzyme
-
Manually annotated by BRENDA team
-
EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space
-
Manually annotated by BRENDA team
-
EP24.15 is secreted
-
Manually annotated by BRENDA team
Bacillus licheniformis N22
-
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
secreted enzyme
-
-
Manually annotated by BRENDA team
Geobacillus sp.
-
-
Manually annotated by BRENDA team
-
intracellular EP24.15 is present throughout the cell, both cytosolic and particulate, with less nuclear localization and no co-localization with either the endoplasmatic reticulum marker calnexin or Golgi marker GM130, overview
Manually annotated by BRENDA team
-
synaptic and fundus membranes in brain
Manually annotated by BRENDA team
-
synaptic and smooth muscle cell membranes in brain
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
exclusively
-
Manually annotated by BRENDA team
-
localized between lipid rafts in the plasma membrane, at the exofacial leaflet of lipid rafts. Biotinylated enzyme is released into the cell media similar to constitutive release
Manually annotated by BRENDA team
-
EP24.15 is associated with the extracellular surface of the cell discernable from the secreted enzyme
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
-
Manually annotated by BRENDA team
-
synaptosomal fraction
Manually annotated by BRENDA team
additional information
-
no activity in membranes of B16F10-Nex2 cells, overview
-
Manually annotated by BRENDA team
additional information
-
wide distribution
-
Manually annotated by BRENDA team
additional information
-
determination of subcellular localization, fractionation and immunohistochemic analysis, overview
-
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
additional information
-
overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium
-
Manually annotated by BRENDA team
additional information
-
secretion of EP24.15 from AT-t20 cells can be stimulated by A23187 and corticotrophin-releasing hormone and blocked by brefeldin A and nocodazole
-
Manually annotated by BRENDA team
additional information
Mus musculus C57BL/6
-
no activity in membranes of B16F10-Nex2 cells, overview
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000 - 70000
-
gel filtration
37053
66000
-
SDS-PAGE
700567
70000
-
gel filtration
37062
75000
-
-
710539
150000
-
gel filtration
37060
184000
-
gel filtration
37066
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 78000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 72985, calculation from nucleotide sequence
?
-
x * 78000
?
-
x * 78000, three-dimensional structure, comparison to EC 3.4.24.16
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 90700, SDS-PAGE
dimer
-
in vitro oligomerization upon S-glutathionylation of the cysteinyl-rich enzyme, the oligomerization has a regulatory function, overview
dimer
Bacillus licheniformis N22
-
2 * 70000, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE
trimer
-
in vitro oligomerization upon S-glutathionylation of the cysteinyl-rich enzyme, the oligomerization has a regulatory function, overview
monomer
-
x * 78300, calculation from nucleotide sequence
additional information
-
interaction of enzyme with type 2 bradykinin receptor and with angiotensin II type I receptor
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
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of recombinant Pz-peptidase A in complex with two phosphinic peptide inhibitors (PPIs) and determination of the crystal structure of these complexes at 1.80-2.00 A resolution is reported. Structure of Pz-peptidase A is closed and globular. It is suggested that collagenous peptide substrates enter the tunnel at the top gateway of the closed Pz-peptidase A molecule, and reactant peptides are released from the bottom gateway after cleavage at the active site located in the center of the tunnel
Geobacillus sp.
Q4W803
Pz peptidase A with bound phosphine peptide inhibitor, 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is incubated with 0.5 mM inhibitor for 24 h at 4 C for complex formation, followed by hanging-drop vapour-diffusion method at 20C for crystallization, mixing of 0.001 ml of protein and reservoir solution, the latter containing 12% w/v PEG 4000, 0.5 M magnesium acetate and 0.1 M Tris-HCl, pH 7.0, 5 days, cryoprotection in 14% w/v PEG 4000, 0.5 M magnesium acetate, 0.1 M TrisHCl, pH 7.0, and 10% v/v 2-propanol, X-ray diffraction structure determination and analysis at 1.80-1.90 A resolution
Geobacillus sp.
-
crystal structure determination
-
hanging-drop vapour diffusion method, recombinant enzyme expressed in Escherichia coli
-
purified recombinant mutant E469R/R498T, hanging drop vapour diffusion method, 4C, 0.001 ml of 10 mg/ml protein is mixed with 0.001 ml of well solution containing 100 mM sodium cacodylate, pH 6.5, 100 mM magnesium acetate, 2 mM 2-mercaptoethanol, and 12-14% w/v polyethylene glycol 6000, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
irreversible inactivation at or below
37066
8
-
unstable above
37063
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
1 h, stable
37060
55
-
1 h, rapid inactivation
37060
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5C or -70C, 3 months, more than 95% of the activity is retained
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Pz peptidase A from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
Geobacillus sp.
-
recombinant Pz peptidases A and B from Escherichia coli strain BL21(DE3) by heat denaturation, anion exchange chromatography and gel filtration, 2.2fold and 8.4fold, respectively
Geobacillus sp.
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
native enzyme from brain
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by glutathione affinity chromatography to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for crystallization, recombinant Pz-peptidase A is purified from an Escherichia coli strain BL21
Geobacillus sp.
Q4W803
overexpression of Pz peptidase A in Escherichia coli strain BL21 (DE3)
Geobacillus sp.
-
Pz peptidases A and B overexpression in Escherichia coli strain BL21(DE3)
Geobacillus sp.
-
expressed in HeLa cells and in Escherichia coli
-
expression of N-terminally HA- or FLAG-tagged enzyme in HEK-293 cells, subcellular localization in the transformed cells, overview
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
cloned from testis and brain
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
2.3 kb cDNA coding for a truncated enzyme of 512 amino acids, displaying the same enzymatic features as endooligopeptidase A
-
gene PA4498, DNA and amino acid sequence determination and analysis
-
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
-
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E469R/R498T
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview
H495N/E469R/R498T
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview
H600A
-
the mutation affects both Km and kcat, the mutant shows changes in the pH-profile, overview
M490R/E469R/R498T
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview
M490R/H495N/E469R
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves TOP and neurolysin sites, overview
M490R/H495N/R498T
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves TOP and neurolysin sites, overview
E502Q
-
inactive mutant enzyme
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
-
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
Y605F
-
considerable decrease in catalytic activity
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
-
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
Y612F
-
marked decrease in catalytic activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thermal unfolding is a two-step process with a major endotherm at a Tm of 64C and a minor endotherm at a Tm of 55C
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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enzyme is involved in extracellular activation of CPI-0004Na prodrug