The Enzyme Database

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Accepted name: nardilysin
Reaction: Hydrolysis of polypeptides, preferably at -Xaa┼Arg-Lys-, and less commonly at -Arg┼Arg-Xaa-, in which Xaa is not Arg or Lys
Other name(s): N-arginine dibasic convertase; NRD-convertase
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: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 292850-69-2
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 (1985) 10541–10545. [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 (1987) 9615–9620. [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 (1994) 2056–2061. [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 (1994) 6078–6082. [DOI] [PMID: 8016118]
[EC created 1995]

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