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
-
neuromedin
- hemopressins
-
arg8-arg9
-
non-at2
-
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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Localization
Localization on EC 3.4.24.16 - neurolysin
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the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin
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additional information
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shorter form of neurolysin, lacking the cleavable mitochondrial targeting sequence, remains in the cytosol
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the membrane-associated enzyme form increases during neuronal differentation and appears to be responsible for the overall augmentation of endopeptidase activity observed during neuronal maturation
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the transfectants exhibit a membrane-associated form of endopeptidase-24.16, the catalytic site of which clearly faces the extracellular domain
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the enzyme is not attached by a glycosyl-phosphatidylinositol anchor in the emembrane, the enzyme can not be released from the membrane upon trypsinolysis
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longer form of neurolysin that contains a cleavable mitochondrial targeting sequence at the N-terminus
truncated enzyme NLN lacking the first 25 aa (region containing the mTP as predicted by TargetP) is not localized in the mitochondria
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additional information
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truncated enzyme NLN lacking the first 25 aa (region containing the mTP as predicted by TargetP) is not localized in the mitochondria
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