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
Search PMC articles PubMed articles NCBI proteins

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

1. Gomez, S., Gluschankof, P., Morel, A. and 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.
2. Gluschankof, P., Gomez, S., Morel, A. and 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.
3. Chesneau, V., Pierotti, A.R., Barré, N., Créminon, C., Tougard, C. and 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.
4. Pierotti, A.R., Prat, A., Chesneau, V., Gaudoux, F., Leseney, A.-M., Foulon, T. and 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)