Nardilysin
| 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 | ||||||||
| |||||||||
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
This enzyme is present rat brain and testis.
References
- ↑ Gomez, S.; Gluschankof, P.; Morel, A.; Cohen, P. (1985). "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". J. Biol. Chem. 260: 10541–10545. PMID 3897221.
- ↑ Gluschankof, P.; Gomez, S.; Morel, A.; Cohen, P. (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". J. Biol. Chem. 262: 9615–9620. PMID 2885328.
- ↑ Chesneau, V.; Pierotti, A.R.; Barré, N.; Créminon, C.; Tougard, C.; Cohen, P. (1994). "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. PMID 8294457.
- ↑ Pierotti, A.R.; Prat, A.; Chesneau, V.; Gaudoux, F.; Leseney, A.-M.; Foulon, T.; Cohen, P. (1994). "N-Arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes". Proc. Natl. Acad. Sci. USA. 91: 6078–6082. doi:10.1073/pnas.91.13.6078. PMID 8016118.
External links
- Nardilysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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