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
-
neuropeptidase
-
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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Subunits
Subunits on EC 3.4.24.16 - neurolysin
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monomer
additional information
hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel, NLN structure analysis, overview
additional information
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hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel, NLN structure analysis, overview
additional information
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three-dimensional structure, comparison to EC 3.4.24.15
additional information
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Gly608 of NEL contributes to the flexibility of the loops formed by residues 600-612, i.e. GHLAGGYDGQYYG, in NEL, overview
additional information
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structural comparison between neurolysin and MMP-9, overview
additional information
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structure analysis and comparisons, modelling, overview