Nardilysin
Nardilysin (EC 3.4.24.61, N-arginine dibasic convertase, NRD-convertase) is an enzyme.[1][2][3][4] 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
| Nardilysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.61 | ||||||||
| CAS number | 292850-69-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
References
- 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. PMID 3897221.
- 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. PMID 2885328.
- 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. PMID 8294457.
- 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. doi:10.1073/pnas.91.13.6078. PMC 44141. PMID 8016118.
External links
- Nardilysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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