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Enzyme Nomenclature
Information on EC 3.4.24.15 - thimet oligopeptidase
for references in articles please use BRENDA:EC3.4.24.15
Word Map on EC 3.4.24.15
- 3.4.24.15
- angiotensin
-
aminopeptidase
-
neuropeptides
-
angiotensin-converting
- neurotensin
-
carboxypeptidase
-
endopeptidases
-
amyloid
- neurolysin
- captopril
- metalloprotease
- 1,10-phenanthroline
- enkephalin
-
thrombospondin
- phosphoramidon
-
natriuretic
-
3.4.24.11
- dynorphins
-
zinc-dependent
-
disintegrin
- enkephalinase
-
opioids
-
i-converting
- bestatin
-
endothelin-converting
-
hexxh
- gcpii
-
enkephalin-containing
- thiorphan
-
post-proline
-
gonadotropin-releasing
-
kininase
-
angiotensin-1-7
- endopeptidase-24.11
-
neuromedin
- adamts1
-
insulin-degrading
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.4.24.15
-
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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
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase; peptides, endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
110639-28-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
37054, 37058, 37063, 652177, 652533, 668185, 668470, 669283, 683672, 683813, 683961, 707401, 708478, 718147
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Pz peptidase A is an intracellular M3 metallopeptidase that is found together with Pz peptidase B in the thermophile Geobacillus collagenovorans MO-1 and recognizes collagen-specific tripeptide units (-Gly-Pro-X-). The peptidases have low homology in their primary structures, but their cleavage patterns towards peptide substrates are similar; Pz peptidase B is an intracellular M3 metallopeptidase that is found together with Pz peptidase A in the thermophile Geobacillus collagenovorans MO-1 and recognizes collagen-specific tripeptide units (-Gly-Pro-X-). The peptidases have low homology in their primary structures, but their cleavage patterns towards peptide substrates are similar. The enzyme thimet oligopeptidase (TOP), a mammalian enzyme, has a similar substrate specificity to the Pz peptidases but shows a much lower identity (14% at most)
evolution
-
Pz peptidase A is an intracellular M3 metallopeptidase that is found together with Pz peptidase B in the thermophile Geobacillus collagenovorans MO-1 and recognizes collagen-specific tripeptide units (-Gly-Pro-X-). The peptidases have low homology in their primary structures, but their cleavage patterns towards peptide substrates are similar; Pz peptidase B is an intracellular M3 metallopeptidase that is found together with Pz peptidase A in the thermophile Geobacillus collagenovorans MO-1 and recognizes collagen-specific tripeptide units (-Gly-Pro-X-). The peptidases have low homology in their primary structures, but their cleavage patterns towards peptide substrates are similar. The enzyme thimet oligopeptidase (TOP), a mammalian enzyme, has a similar substrate specificity to the Pz peptidases but shows a much lower identity (14% at most)
-
malfunction
-
inhibition of EP24.15 activity with a specific inhibitor augments the steroid-induced luteinizing hormone increase in ovariectomized rats
malfunction
-
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
-
thimet oligopeptidase is a metallo-oligopeptidase that participates in the intracellular metabolism of peptides
metabolism
-
EP24.15 is the main enzyme of luteinizing hormone-releasing hormone, i.e. LHRH, metabolism as the prime mediator of LHRH-I degradation in both the brain and periphery
metabolism
-
enzyme activity changes in the brain might play important role in the balance of neuropeptide level correlated with cocaine effects
metabolism
relationship between enzyme expression and laminar shear stress, a haemodynamic force associated with endothelium-mediated vascular homeostasis, shear stress is a positive regulator of thimet oligopeptidase in vascular endothelial cells activating the TOP promoter. Shear stress-dependent induction of the enzyme may lower MHC1 expression
metabolism
-
relationship between enzyme expression and laminar shear stress, a haemodynamic force associated with endothelium-mediated vascular homeostasis, shear stress is a positive regulator of thimet oligopeptidase in vascular endothelial cells activating the TOP promoter. Shear stress-dependent induction of the enzyme may lower MHC1 expression
metabolism
-
elevations in the levels of thimet oligopeptidase, Ang-(1-7), and of receptor Mas transcripts are observed in chronically stimulated epileptic rats
metabolism
-
elevations in the levels of thimet oligopeptidase, Ang-(1-7), and of receptor Mas transcripts are observed in chronically stimulated epileptic rats; enzyme activity changes in the brain might play important role in the balance of neuropeptide level correlated with cocaine effects
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physiological function
-
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
-
involvement of EP24.15 in the modulation of hypothalamic luteinizing hormone-releasing hormone, LHRH, neuronal function
physiological function
-
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
-
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
-
many roles of EP24.15 in the metabolism of neuropeptides and in cell regulation, overview
physiological function
-
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
-
the enzyme is implicated in the processing of opioid peptides, including, beta-neoendorphin, alpha-neoendorphin, dynorphin 1-8 and nociceptin/orphanin, modifications on TOP activity can potentially result in alterations in the metabolism of these neuropeptides and in vivo could be related to cocaine addiction
physiological function
-
angiotensin-(1-7) is the main metabolite of angiotensin I in rat hippocampi, and thimet oligopeptidase is the main enzyme involved in the generation of Ang-(1-7), which binds to the receptor Mas. In the central nervous system specifically, the heptapeptide is involved in learning and memory processes that occur in central limbic regions, such as the hippocampus
physiological function
-
the thiol-rich enzyme enzyme is able to interact with the structure of myoglobin and horseradish peroxidase and acts as a reducing agent for the H2O2-promoted oxidized forms of these heme proteins
physiological function
-
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
-
angiotensin-(1-7) is the main metabolite of angiotensin I in rat hippocampi, and thimet oligopeptidase is the main enzyme involved in the generation of Ang-(1-7), which binds to the receptor Mas. In the central nervous system specifically, the heptapeptide is involved in learning and memory processes that occur in central limbic regions, such as the hippocampus; the enzyme is implicated in the processing of opioid peptides, including, beta-neoendorphin, alpha-neoendorphin, dynorphin 1-8 and nociceptin/orphanin, modifications on TOP activity can potentially result in alterations in the metabolism of these neuropeptides and in vivo could be related to cocaine addiction
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additional information
-
expression and activity of thimet oligopeptidase are increased in the hippocampus in the chronic phase of subjects with temporal lobe epilepsy, but not in the silent phase. In addition, decreased enzyme distribution is also visualized by immunohistochemistry. These alterations can be related to a failure in the mechanisms involved in clearance of inflammatory peptides in the hippocampus, suggesting an accumulation of potentially harmful substances in nervous tissue such as amyloid beta, bradykinin, and antigenic peptides
additional information
-
expression and activity of thimet oligopeptidase are increased in the hippocampus in rats during the acute phase of pilocarpine-induced epilepsy model, but not in the silent phase. In addition, decreased enzyme distribution is also visualized by immunohistochemistry. These alterations can be related to a failure in the mechanisms involved in clearance of inflammatory peptides in the hippocampus, suggesting an accumulation of potentially harmful substances in nervous tissue such as amyloid beta, bradykinin, and antigenic peptides
additional information
-
H2O2 mechanism of enzyme oxidation by hydrogen peroxide, and proposed mechanism of TOP participation in the redox cycling of myoglobin, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
fluorogenic substrate
-
-
?
(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
-
-
-
?
(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
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH + H2O
?
-
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-yl)actayl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH + H2O
?
-
-
-
-
?
(Gly-Pro-Leu)n
Gly-Pro-Leu
-
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
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
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)
-
16% cleavage at P-Y bond, 40% cleavage at Y-Q bond, 44% cleavage at R-R
-
?
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-FFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GASP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GDSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GESP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFAP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFDP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFEP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFFP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFHP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFIP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFLP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFNP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFPP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFQP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFRP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSA + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSD + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSE + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSF + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSL + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSN + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + ARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-GFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
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)
-
-
-
?
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRSSRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSPFRS + SRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
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)
-
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)
-
-
-
?
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + HRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + NRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + QRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSQ + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSR + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSS + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + REQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
-
-
?
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
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)
-
-
-
?
(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)
-
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)
-
-
-
?
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GISP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GLSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GNSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GPSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GQSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GRSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GSSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-HFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-KPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LYENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(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)
-
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)
-
-
-
?
(o-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-Phe-Arg-Lys-(dinitrophenyl-proline) + H2O
(o-aminobenzoyl)-Phe-Arg + Lys-(dinitrophenyl-proline)
-
-
-
?
(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)
-
-
-
?
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
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)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
(o-aminobenzoyl)-RPPGFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
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)
-
-
-
?
2-aminobenzoyl-GFSHFRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-GFSH + FRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
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)
-
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)
-
-
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
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
4-phenylazobenzyloxycarbonyl-Pro + Leu-Gly-Pro-D-Arg
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-2,4-dinitrophenyl + H2O
?
-
fluorogenic substrate
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol + H2O
?
-
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
?
-
-
?
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin + H2O
?
-
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
?
-
-
-
?
7-methoxycoumaryl-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumatin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
aminobenzyl-Ala-Gly-Leu-Ala-nitrobenzylamide
aminobenzyl-Ala-Gly + Leu-Ala-nitrobenzylamide
-
weak
-
?
amyloid precursor protein-derived substrate
peptide fragments
-
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
-
?
benzoyl-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Arg + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Asp-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Asp + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Lys-Arg + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
-
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
-
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
-
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
-
-
?
GFGDLKSPAGLQV + H2O
GFGDLK + SPAGLQV
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation elongation factor 1beta2
-
-
?
IHSLPPEGKLG
IHSLPPE + GKLG
-
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
-
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
-
-
-
LVVYPWTQRY + H2O
?
-
0.72% of the activity with bradykinin, cleavage sites: LVVYP-/-W-/-T-/-Q-/-RY
-
?
major histocompatibility complex class I-presented antigenic peptides + H2O
?
-
by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Arg-N-(2,4-dinitrophenyl)ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Val-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
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
propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met
propionyl-Gly-Ser-Pro-(farnesyl-Cys) + Val-Leu-Met
-
-
-
?
pTLRTKL + H2O
phospho-Thr-Leu-Arg + L-tyrosine + Lys-Leu
-
at 10% of the rate with RPPGF-SP-FR
-
-
?
PVNFKFLSH + H2O
?
-
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
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ?
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(1–5). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor
-
?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
-
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
-
-
-
succinyl-Ala-Ala-Ala-4-nitroanilide
succinyl-Ala-Ala + Ala-4-nitroanilide
-
weak
-
?
succinyl-Ala-Ala-Phe-4-nitroanilide
succinyl-Ala-Ala + Phe-4-nitroanilide
-
weak
-
?
succinyl-Ala-Ala-Val-4-nitroanilide
succinyl-Ala-Ala + Val-4-nitroanilide
-
weak
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
Tyr-Gly-Gly-Phe-Leu + Arg-Lys-Tyr-Pro
-
beta-neoendorphin
-
?
VVYPW-TQ-RY-KL + H2O
VVYPW + Thr-Gln + Arg-Tyr + Lys-Leu
-
at 9% of the rate with RPPGF-SP-FR
-
-
?
VVYPWTQRY + H2O
?
-
10.6% of the activity with bradykinin, cleavage sites: VVYPW-/-T-/-Q-/-RY
-
?
(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
-
a fluorescent-quenched substrate
-
-
?
(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
a fluorescent-quenched substrate
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
85% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
i.e. Pz-peptide
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
i.e. Pz-peptide
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
-
-
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11
-
-
-
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11
-
-
-
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
cleavage sites: Pro4-Gln5, Phe8-Gly9 and Phe7-Phe8
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, Phe8-Gly9
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
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
-
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
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
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
-
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
-
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
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II, cleavage site: Tyr4-Ile5
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II, cleavage site: Tyr4-Ile5
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
-
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
-
-
-
?
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-Ala-Phe-p-aminobenzoate
-
-
-
?
Bradykinin + H2O
?
-
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
-
-
?
Collagen + H2O
?
-
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
?
-
the enzyme recognizes the specific sequence Gly-Pro-Xaa of in collagen
-
-
?
Collagen + H2O
?
-
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
?
-
the enzyme recognizes the specific sequence Gly-Pro-Xaa of in collagen
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
-
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
-
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
-
-
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
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
-
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
-
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
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
-
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
-
-
-
-
?
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
-
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
-
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
-
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
-
-
-
-
?
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
-
i.e. neurotensin
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
-
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
-
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
-
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-(1–5)
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
-
-
-
-
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
i.e. dynorphin A(1-8)
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
i.e. dynorphin A(1-8)
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
-
dynorphin 1-17
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
-
dynorphin 1-17
-
-
?
additional information
?
-
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro
-
-
-
additional information
?
-
-
no cleavage of denatured collagen, hemoglobin and casein
-
-
-
additional information
?
-
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro
-
-
-
additional information
?
-
-
no cleavage of denatured collagen, hemoglobin and casein
-
-
-
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
-
additional information
?
-
-
no activity with Gly-Phe-Leu-Gly-Phe-Ile-Gly-Phe-Leu
-
-
-
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
-
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
?
-
-
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
?
-
-
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 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
?
-
-
the enzyme is able to act as a reducing agent in the peroxidase cycle of myoglobin and horseradish peroxidase. The enzyme also prevents the formation of tryptophanyl radical in myoglobin challenged by H2O2
-
-
-
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
?
-
-
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
?
-
-
substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
-
additional information
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
-
additional information
?
-
-
substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
-
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
?
-
-
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
?
-
-
cleaves preferentially bonds on the carboxyl side of hydrophobic amino acids
-
-
-
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
?
-
-
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
?
-
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, overview
-
-
-
additional information
?
-
-
cleavage sites of wild-type and mutant enzymes, 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
?
-
-
phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
-
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
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation elongation factor 1beta2
-
-
?
IHSLPPEGKLG
IHSLPPE + GKLG
-
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
-
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
-
-
-
major histocompatibility complex class I-presented antigenic peptides + H2O
?
-
by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ?
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(1–5). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor
-
?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
-
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
-
-
-
Bradykinin + H2O
?
-
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
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
-
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
-
gonadotropin-releasing hormone, the enzyme degrades gonadotropin-releasing hormone, GnRH, by cleaving the central Tyr5-Gly6 bond
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
-
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
-
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 able to act as a reducing agent in the peroxidase cycle of myoglobin and horseradish peroxidase. The enzyme also prevents the formation of tryptophanyl radical in myoglobin challenged by H2O2
-
-
-
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
?
-
-
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 angiogenesis and tumor growth, overview
-
-
-
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
?
-
-
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
?
-
-
proposed role in formation of enkephalins
-
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Zinc
Zn2+
additional information
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
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)
Zinc
-
contains 2 gatom of zinc per mol of enzyme, one catalytic zinc and one structural zinc
Zn2+
-
catalytic zinc, the binding site is rather distinct from the calmodulin/Ca2+ binding site
Zn2+
-
second step of structural unfolding results in complete loss of catalytic Zn2+
additional information
-
Pz peptidase A is an intracellular M3 metallopeptidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
angiotensin I
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
angiotensin II
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
Arg-Pro-Ala-Gly-Phe-(3-aminopropanoyl)-Pro-Phe-Arg
-
no degradation by EC 3.4.24.15
Arg-Pro-Pro-Ala-Phe-(3-aminopropanoyl)-Pro-Phe-Arg
-
low degradation by EC 3.4.24.15
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
IC50: 0.007 mM, degradation by EC 3.4.24.15
ATP
-
Zn2+ at the active center of the enzyme is the target for the ATP binding to the enzyme leading to the peptidase inhibition and to the enzyme autophosphorylation
bradykinin
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
dynorphin A1-13
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
L-phospho-Thr-Leu-Arg-Thr-Lys-Leu
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
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
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-p-aminobenzoate
-
specific inhibitor JA-2
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-4-aminobenzoate
-
specific inhibitor JA-2
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)-carboxyl-2-phenylethyl]-Ala-Ala-Phe-4-amino-benzoate
-
i.e. cFP-AAF-pAB, an active site-directed inhibitor
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
VVYPW-phenylThr-Gln-Arg-Tyr
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Ser
-
specific for thimet oligopeptidase
Z-(D,L)-Phe-PSI[PO2CH2]-(D,L)-Ala-Lys-Tyr
-
specific for thimet oligopeptidase
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
LVVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
LVVYPWTQRY
-
comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme
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-Aib-Tyr-4-aminobenzoate
-
specific TOP enzyme inhibitor JA-2
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
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
-
additional information
-
phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
cocaine
-
cocaine treatment causes an increase in the ventral striatum in enzyme specific activity and enzyme relative mRNA amount determined by real time RT-PCR
GSSG
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, maximal activity by partial S-glutathionylation, overview
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
2-mercaptoethanol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of 2-mercaptoethanol
dithiothreitol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of dithiothreitol
dithiothreitol
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of dithiothreitol
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
-
additional information
-
the mdpA gene is induced in the presence of XPro dipeptides, such as Phe-Pro, Gly-Pro
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0014
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0012 - 0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
0.0045
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.003
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.001
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0042
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0166
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0225
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00071
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0068
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0052
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00072
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00099
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00038
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00027
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0149
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0053
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0076
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.004
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.037
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.018
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.002
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0139
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.119
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0019
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0126
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0044
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.131
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0203
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0048
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0005
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00057
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0022
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00019
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.007
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0085
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.005
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0073
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0075
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0022
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0005
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0033
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0019
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0007
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0017
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0018
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0007
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0015
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0012
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0023
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0022
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0021
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0006
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0048
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0028
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0099
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0036
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00016
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00082
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00078
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0102
(ortho-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.021
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0028
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.114
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.007
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0071
(ortho-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.064
(ortho-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.036
(ortho-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.015
(ortho-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0124
(ortho-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0121
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0123
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)
pH and temperature not specified in the publication
additional information
additional information
-
kinetics of wild-type and mutant TOP
-
0.014
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.024
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
wild-type, 23°C, pH 7.8
0.034
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y612F, 23°C, pH 7.8
0.037
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605F, 23°C, pH 7.8
0.0012
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
wild-type, 23°C, pH 7.8
0.0025
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G599A, 23°C, pH 7.8
0.0026
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G604A, 23°C, pH 7.8; mutant Y612F, 23°C, pH 7.8
0.0029
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A, 23°C, pH 7.8; mutant G603P, 23°C, pH 7.8
0.0031
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.0042
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605F, 23°C, pH 7.8
0.005
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G611A, 23°C, pH 7.8
0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A/G604A, 23°C, pH 7.8
0.0015
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0022
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0043
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
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, 23°C
0.00013
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23°C, presence of 1.5 M urea
0.00048
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23°C, presence of 2.5 M urea
0.00127
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
-
pH 7.8, 23°C, presence of 3.5 M urea
0.00401
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A, 23°C, pH 7.8
0.00408
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G599A, 23°C, pH 7.8
0.00543
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A/G604A, 23°C, pH 7.8
0.00643
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603P, 23°C, pH 7.8
0.0067
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G611A, 23°C, pH 7.8
0.00788
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
wild-type, 23°C, pH 7.8
0.0081
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605FY612F, 23°C, pH 7.8