3.4.24.16: neurolysin
This is an abbreviated version!
For detailed information about neurolysin, go to the full flat file.
Word Map on EC 3.4.24.16
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3.4.24.16
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bradykinin
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metallopeptidase
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metalloendopeptidase
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dynorphins
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pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
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hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
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molecular biology
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pharmacology
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medicine
- 3.4.24.16
- bradykinin
- metallopeptidase
- metalloendopeptidase
- dynorphins
- pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
- hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
- molecular biology
- pharmacology
- medicine
Reaction
Preferential cleavage in neurotensin: Pro10-/-Tyr =
Synonyms
endopeptidase 24.16, endopeptidase 24.16B, endopeptidase 3.4.24.16, EP 24.16, ep24.16, EP24.16c, EP24.16m, MEP, Microsomal endopeptidase, mitochondrial peptidase, MOP, More, NEL, neurolisin, neurolysin, neurotensin endopeptidase, neurotensin-cleaving enzyme, Nln, oligopeptidase M, peptidase, neurotensin endo, peptidase, neurotensin endo-, SABP, soluble angiotensin II-binding protein, Soluble angiotensin-binding protein, thimet oligopeptidase II, thimet peptidase II
ECTree
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General Information
General Information on EC 3.4.24.16 - neurolysin
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evolution
malfunction
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brain membranes of mice lacking neurolysin are nearly devoid of the non-AT1, non-AT2 angiotensin binding site
metabolism
a network of proteases may be required for complete degradation of peptides localized in mitochondria. Mechanism of peptide binding
physiological function
additional information
neuropeptidases specialize in the hydrolysis of the small bioactive peptides that play a variety of signaling roles in the nervous and endocrine systems. Neuropeptidase neurolysin helps control the levels of the dopaminergic circuit modulator neurotensin and is a member of a fold group that includes the antihypertensive target angiotensin converting enzyme
physiological function
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the enzyme is involved in peptidergic systems that play a role in pathogenesis of stroke and resistance to ischemic injury and/or post-stroke brain recovery. Neurolysin may play a role in processes modulating the brain's response to stroke and its recovery after stroke
physiological function
the enzyme serves as non-AT1, non-AT2 binding site for angiotensins in the rodent brain and testis, the binding of neurolysin is inhibited by enzyme substrates, peptide screening and competitive binding assays, detailed overview
physiological function
neurolysin cleaves mitochondrial targeting peptides
physiological function
Nln secreted from B16F10-Nex2 melanoma cells might be able control angiogenesis. Nln hydrolyses several substrates that are affected by brain injury
physiological function
peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders. The enzyme is linked to neuronal cell death. Significant increase (about twofold) in quantity and activity of membrane Nln in ischemia-affected parts of the mouse brain. Enzyme Nln may play a role in processes modulating the brain's response to stroke
physiological function
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the enzyme serves as non-AT1, non-AT2 binding site for angiotensins in the rodent brain and testis, the binding of neurolysin is inhibited by enzyme substrates, peptide screening and competitive binding assays, detailed overview
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physiological function
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Nln secreted from B16F10-Nex2 melanoma cells might be able control angiogenesis. Nln hydrolyses several substrates that are affected by brain injury
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hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel. The enclosed cavity structure restricts substrate length. hNLN contains the conserved HExxH zinc-binding motif, which is a signature of the MA clan of metallopeptidases. In hNLN, the residues His474, His478 and Glu503 take part in the coordination of the catalytic zinc ion. NLN structure analysis, mechanism of peptide binding, detailed overview. The large hydrophobic side chains of Ile12NT2 and Leu13NT2 may be attracted by the strong hydrophobicity of the S3' (Leu558 and Phe599) and aromatic S4' residues (Phe226, Tyr339). A single hydrogen bond between Tyr610 and Tyr11NT2 contributes to the recognition of the peptide's main chain. In addition, Arg554 (S4') offers an anchor point for the carboxyl-terminus of NT2 via salt bridge formation. Overall, peptide stabilization occurs through mainchain interactions with the observed subsites within the catalytic cavity but with these interactions not imposing a strict substrate specificity
additional information
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hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel. The enclosed cavity structure restricts substrate length. hNLN contains the conserved HExxH zinc-binding motif, which is a signature of the MA clan of metallopeptidases. In hNLN, the residues His474, His478 and Glu503 take part in the coordination of the catalytic zinc ion. NLN structure analysis, mechanism of peptide binding, detailed overview. The large hydrophobic side chains of Ile12NT2 and Leu13NT2 may be attracted by the strong hydrophobicity of the S3' (Leu558 and Phe599) and aromatic S4' residues (Phe226, Tyr339). A single hydrogen bond between Tyr610 and Tyr11NT2 contributes to the recognition of the peptide's main chain. In addition, Arg554 (S4') offers an anchor point for the carboxyl-terminus of NT2 via salt bridge formation. Overall, peptide stabilization occurs through mainchain interactions with the observed subsites within the catalytic cavity but with these interactions not imposing a strict substrate specificity