| EC |
3.4.24.16 |
| Accepted name: |
neurolysin |
| Reaction: |
Preferential cleavage in neurotensin: Pro10┼Tyr |
| Other name(s): |
neurotensin endopeptidase; endopeptidase 24.16; endo-oligopeptidase B (proline-endopeptidase) |
| Comments: |
No absolute requirement for a prolyl bond: the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do. In peptidase family M3 (thimet oligopeptidase family) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 149371-24-4 |
| References: |
| 1. |
Checler, F., Vincent, J.P. and Kitabgi, P. Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes. J. Biol. Chem. 261 (1986) 11274–11281. [PMID: 3525564] |
| 2. |
Barelli, H., Vincent, J.-P. and Checler, F. Peripheral inactivation of neurotensin. Isolation and characterization of a metallopeptidase from rat ileum. Eur. J. Biochem. 175 (1988) 481–489. [DOI] [PMID: 3409880] |
| 3. |
Checler, F., Barelli, H. and Vincent, J.-P. Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies. Biochem. J. 257 (1989) 549–554. [PMID: 2649078] |
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| [EC 3.4.24.16 created 1989] |
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