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Literature summary extracted from

  • Barrett, A.J.; Dando, P.M.
    Neurolysin (2004), Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press, 1, 356-360.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.16 additional information not activated by thiol compounds Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.16
-
 Mus musculus
3.4.24.16
-
 Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.16
-
 Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.16 1,10-phenanthroline
-
 Rattus norvegicus
3.4.24.16 EDTA
-
 Rattus norvegicus
3.4.24.16 HONHCO-CH2-CH(CH2-C6H5)CO-Ile-Ala potent and selective inhibitor of neurolysin Rattus norvegicus
3.4.24.16 additional information inhibitor of neurolysin potentiates the neurotensin-induced anti-nociception Mus musculus
3.4.24.16 Pro-Ile selective inhibitor of neurolysin, inhibition by milimolar concentrations Rattus norvegicus
3.4.24.16 Pro-Phe-PSI(PO2CH2)Gly-Pro potent and selective inhibitor of neurolysin Rattus norvegicus
3.4.24.16 Pro-Phe-PSI(PO2CH2)Leu-Pro-NH2 potent and selective inhibitor of neurolysin Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.16 cytosol
-
 Sus scrofa 5829
-
3.4.24.16 cytosol shorter form of neurolysin, lacking the cleavable mitochondrial targeting sequence, remains in the cytosol Rattus norvegicus 5829
-
3.4.24.16 mitochondrion
-
 Sus scrofa 5739
-
3.4.24.16 mitochondrion longer form of neurolysin that contains a cleavable mitochondrial targeting sequence at the N-terminus Rattus norvegicus 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.16 78000
-
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.16 Homo sapiens
-
-
-
3.4.24.16 Mus musculus
-
-
-
3.4.24.16 Oryctolagus cuniculus
-
-
-
3.4.24.16 Rattus norvegicus
-
-
-
3.4.24.16 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.16
-
 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.16 brain
-
 Homo sapiens
-
3.4.24.16 brain
-
 Rattus norvegicus
-
3.4.24.16 brain
-
 Sus scrofa
-
3.4.24.16 heart
-
 Rattus norvegicus
-
3.4.24.16 heart
-
 Sus scrofa
-
3.4.24.16 kidney
-
 Rattus norvegicus
-
3.4.24.16 kidney
-
 Sus scrofa
-
3.4.24.16 liver
-
 Rattus norvegicus
-
3.4.24.16 liver
-
 Sus scrofa
-
3.4.24.16 lung
-
 Rattus norvegicus
-
3.4.24.16 lung
-
 Sus scrofa
-
3.4.24.16 spleen
-
 Rattus norvegicus
-
3.4.24.16 spleen
-
 Sus scrofa
-
3.4.24.16 testis
-
 Rattus norvegicus
-
3.4.24.16 testis
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.16 dynorphin A(1-17) + H2O
-
 Rattus norvegicus ?
-
 ?
3.4.24.16 neurotensin + H2O cleavage at the Pro-Tyr bond Rattus norvegicus ?
-
 ?
3.4.24.16 Pz-Pro-Leu-Gly-Pro-D-Arg + H2O
-
 Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.16 monomer
-
 Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
3.4.24.16 endopeptidase 24.16
-
 Rattus norvegicus
3.4.24.16 Microsomal endopeptidase
-
 Rattus norvegicus
3.4.24.16 oligopeptidase M
-
 Rattus norvegicus
3.4.24.16 soluble angiotensin II-binding protein
-
 Rattus norvegicus
3.4.24.16 thimet oligopeptidase II neurolysin is most likely to be confused with thimet oligopeptidase II, but it is distinguished by its lack of activation by thiol compounds, inhibition by millimolar concentrations of Pro-Ile, cleavage of neurotensin at the Pro-Tyr bond, and different mobility in column chromatography Rattus norvegicus