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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.16 neurolysin

Purification

Purification on EC 3.4.24.16 - neurolysin

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a two-step purification procedure based on the molecular size and isoelectric point of the photoradiolabeled binding protein is conducted. Purified samples are subjected to two-dimensional gel electrophoresis followed by mass spectrometry identification of proteins in the two-dimensional gel sections containing radioactivity. LC-MS/MS analysis reveal protein candidates, of which the most abundant are immunoprecipitated after photoradiolabeling. Immunoprecipitation studies indicate that the angiotensin binding site is the membrane-bound variant of metalloendopeptidase neurolysin
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partial
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recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by glutathione affinity chromatography to homogeneity
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration to homogeneity, large scale production of rNln
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
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