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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Natural Substrates Products
Natural Substrates Products on EC 3.4.24.16 - neurolysin
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REACTION DIAGRAM
FSTSAQNN + H2O
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octMdh1, Oct1 generated octapeptide from Mus musculus
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GlpLYENKPRRPYIL + H2O
GlpLYENKPRRP + YIL
neurotensin, secreted human neuropeptide
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MFLTRFVGRRFLAAASARS + H2O
MFLTR + FVG + RRFL + 2 L-Ala + ASA + RS
pL29, presequence from Arabidopsis thaliana
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MFRRPVLQVLRQFVRH + H2O
MFR + RPVL + QVLR + QFVRH
pSSBP, human presequence
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neurotensin + H2O
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neurolysin regulates the amount of bioactive peptide neurotensin, which functions in the modulation of central dopaminergic and cholinergic circuits, thermoregulation, intestinal motility, and blood pressure regulation. In cancer cells, neurotensin accelerates cell progression
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the enzyme is involved in the inactivation of numerous neuropeptides
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additional information
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the enzyme contributes to the catabolism of neurotensin in the dog intestine
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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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possible implication of the enzyme in the specific degradation of neurotensin and other peptide neurotransmitters in the synaptic cleft
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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 secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin. The neuronal membrane-associated activity would be responsible for the physiological inactivation of the peptide either in the synaptic cleft, beside the neurotensin receptors, or inside early endosomal compartments in which receptor-ligand complexes would have been internalized
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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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membrane-bound variant of neurolysin functions as the non-angiotensin Type 1 (non-AT1), non-AT2 Angiotensin binding site
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additional information
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angiotensin I, dynorphin A(1-8) and metorphamide are no substrates of neurolysin
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additional information
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Nln hydrolyses several substrates that are affected by brain injury
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additional information
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Nln hydrolyses several substrates that are affected by brain injury
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additional information
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the enzyme can participate in the physiological inactivation of neurotensin
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additional information
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EC 3.4.24.16 and EC 3.4.24.15 are responsible for the inactivation of neurotensin, somatostatin, and other neuropeptides in the brain
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additional information
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the enzyme is likely involved in the physiological termination of the neurotensinergic signal in the central nervous system and in the gastrointestinal tract
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additional information
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the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15
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additional information
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the enzyme is involved in the inactivation of numerous neuropeptides
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