3.4.24.15: thimet oligopeptidase
This is an abbreviated version!
For detailed information about thimet oligopeptidase, go to the full flat file.
Word Map on EC 3.4.24.15
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3.4.24.15
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angiotensin
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aminopeptidase
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endothelial
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angiotensin-converting
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neuropeptides
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metastasis
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timp
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mmp-9
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metalloproteinase
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neurotensin
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carboxypeptidase
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thrombospondin
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chondrocytes
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cartilage
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osteoarthritis
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endopeptidases
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neurolysin
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disintegrin
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transwell
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enkephalin
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captopril
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natriuretic
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1,10-phenanthroline
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phosphoramidon
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zinc-dependent
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dynorphins
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aggrecan
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bestatin
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ace2
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enkephalinase
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adam17
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hexxh
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i-converting
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gcpii
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endothelin-converting
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thiorphan
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endopeptidase-24.11
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lhrh
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insulin-degrading
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angiotensin-1-7
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post-proline
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adamts1
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enkephalin-containing
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medicine
- 3.4.24.15
- angiotensin
- aminopeptidase
- endothelial
-
angiotensin-converting
- neuropeptides
- metastasis
- timp
- mmp-9
- metalloproteinase
- neurotensin
- carboxypeptidase
- thrombospondin
- chondrocytes
- cartilage
- osteoarthritis
- endopeptidases
- neurolysin
-
disintegrin
-
transwell
- enkephalin
- captopril
-
natriuretic
- 1,10-phenanthroline
- phosphoramidon
-
zinc-dependent
- dynorphins
- aggrecan
- bestatin
- ace2
- enkephalinase
- adam17
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hexxh
-
i-converting
- gcpii
-
endothelin-converting
- thiorphan
- endopeptidase-24.11
- lhrh
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insulin-degrading
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angiotensin-1-7
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post-proline
- adamts1
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enkephalin-containing
- medicine
Reaction
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues =
Synonyms
BIE, bradykinin-inactivating endopeptidase, EC 3.4.22.19, EC 3.4.99.31, endo-oligopeptidase A, endooligopeptidase A, endopeptidase 24-15, endopeptidase 24.15, endopeptidase EC 3.4.24.15, EOPA, EP 24.15, EP24.15, MdpA, metallo-dipeptidase aeruginosa, metalloendopeptidase 24.15, metalloendopeptidase EC 3.4.24.15, metallopeptidase, More, MP78, neutral endopeptidase 24.15, PA4498, peptidase, thimet oligo-, Pz peptidase A, Pz peptidase B, Pz-peptidase, Pz-peptidase A, soluble metallo-endopeptidase, soluble metallopeptidase, thimet oligopeptidase, thimet peptidase, thimet-oligopeptidase, thiol-dependent metalloendopeptidase, THOP1, TOP, Top1, Top2
ECTree
3.4.24.15 thimet oligopeptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.15 - thimet oligopeptidase
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NATURAL SUBSTRATE 
NATURAL 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
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
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intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from peptidylprolyl isomerase A
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-
?
GFGDLKSPAGLQV + H2O
GFGDLK + SPAGLQV
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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
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-
?
IHSLPPEGKLG
IHSLPPE + GKLG
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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
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-
?
KDIEDVFYKY
KDIEDVF + YKY
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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
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-
?
major histocompatibility complex class I-presented antigenic peptides + H2O
?
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by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
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?
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 + ?
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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
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?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
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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
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-
?
bradykinin + H2O
?
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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
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-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
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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
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gonadotropin-releasing hormone, the enzyme degrades gonadotropin-releasing hormone, GnRH, by cleaving the central Tyr5-Gly6 bond
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-
?
additional information
?
-
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the enzyme is active in inactivation of neuropeptides, biological relevance, overview
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-
?
additional information
?
-
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enzyme is involved in degradation of proteasomal products of 9-17 residues
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-
?
additional information
?
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the enzyme cleaves several bioactive peptides at sites similar or different from neurolysin, EC 3.4.24.16
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-
?
additional information
?
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the enzyme is active in inactivation of neuropeptides, biological relevance, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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the enzyme is active in inactivation of neuropeptides, biological relevance, overview
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-
?
additional information
?
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the enzyme is involved in angiogenesis and tumor growth, overview
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-
?
additional information
?
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the enzyme is involved in angiogenesis and tumor growth, overview
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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proposed role in formation of enkephalins
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-
?
additional information
?
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enzyme is involved in degradation of proteasomal products of 9-17 residues
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?
additional information
?
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enzyme modulates intracellular, peptidergic signaling cascades through type 2 bradykinin receptor
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-
?
additional information
?
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enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, overview
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-
?
additional information
?
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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
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?
