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
-
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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Cloned
Cloned on EC 3.4.24.16 - neurolysin
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expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha
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expression of neurolysin gene fron brain ligated to the C-terminal half of the alpha-agglutinin gene with a FLAG tag sequence in Saccharomyces cerevisiae at the cell surface, construction of a molecular displaying plasmid
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expression of the FLAG-tagged brain enzyme in Saccharomyces cerevisiae strain BJ2168 on the cell surface, subcloning in Escherichia coli strain DH5alpha
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene NLN
gene NLN, sequence comparisons and phylogenetic tree, transient transfection of HeLa cells with C-terminally myc-tagged full-length human NLN (hNLN1-704) followed by immunolocalization reveals a typical mitochondrial pattern. Transfection with a construct lacking the first 25 aa (region containing the mTP as predicted by TargetP) abolishes the mitochondrial localization of hNLN
overexpressed in human kidney cells, HK293 cells. The transfectants exhibit a membrane-associated form of endopeptidase-24.16, the catalytic site of which clearly faces the extracellular domain. Transfected cells are unable to secrete the enzyme
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recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli