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Nardilysin (EC 3.4.24.61, N-arginine dibasic convertase, NRD-convertase) is an enzyme. This enzyme catalyses the following chemical reaction

Hydrolysis of polypeptides, preferably at -Xaa-Arg-Lys-, and less commonly at -Arg-Arg-Xaa-, in which Xaa is not Arg or Lys

This enzyme is present rat brain and testis.

References

1. Gomez S, Gluschankof P, Morel A, Cohen P (September 1985). "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". The Journal of Biological Chemistry. 260 (19): 10541–5. doi:10.1016/S0021-9258(19)85118-9. PMID 3897221.
2. Gluschankof P, Gomez S, Morel A, Cohen P (July 1987). "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". The Journal of Biological Chemistry. 262 (20): 9615–20. doi:10.1016/S0021-9258(18)47978-1. PMID 2885328.
3. Chesneau V, Pierotti AR, Barré N, Créminon C, Tougard C, Cohen P (January 1994). "Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues". The Journal of Biological Chemistry. 269 (3): 2056–61. doi:10.1016/S0021-9258(17)42134-X. PMID 8294457.
4. Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P (June 1994). "N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 6078–82. Bibcode:1994PNAS...91.6078P. doi:10.1073/pnas.91.13.6078. PMC 44141. PMID 8016118.

External links

• Nardilysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.24