EC 3.4.24.61 - Nardilysin

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.24.61

Names

Accepted name:
nardilysin
Other names:
N-arginine dibasic convertase
NRD-convertase
Systematic name:
-

Reaction

Cofactor

Comments:

Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00130
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016919
CAS Registry Number: 157906-54-2
UniProtKB/Swiss-Prot:

References

  1. Gomez, S., Gluschankof, P., Morel, A. and Cohen, P.
    The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes.
    J. Biol. Chem. 260: 10541-10545 (1985). [PMID: 3897221]
  2. Gluschankof, P., Gomez, S., Morel, A. and Cohen, P.
    Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex.
    J. Biol. Chem. 262: 9615-9620 (1987). [PMID: 2885328]
  3. Chesneau, V., Pierotti, A.R., Barré, N., Créminon, C., Tougard, C. and Cohen, P.
    Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues.
    J. Biol. Chem. 269: 2056-2061 (1994). [PMID: 8294457]
  4. Pierotti, A.R., Prat, A., Chesneau, V., Gaudoux, F., Leseney, A.-M., Foulon, T. and Cohen, P.
    N-Arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.
    Proc. Natl. Acad. Sci. USA 91: 6078-6082 (1994). [PMID: 8016118]

[EC 3.4.24.61 created 1995]