Biology:Nardilysin

From HandWiki
Nardilysin
Identifiers
EC number3.4.24.61
CAS number292850-69-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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

  1. "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". The Journal of Biological Chemistry 260 (19): 10541–5. September 1985. doi:10.1016/S0021-9258(19)85118-9. PMID 3897221. 
  2. "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. July 1987. doi:10.1016/S0021-9258(18)47978-1. PMID 2885328. 
  3. "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. January 1994. doi:10.1016/S0021-9258(17)42134-X. PMID 8294457. 
  4. "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. June 1994. doi:10.1073/pnas.91.13.6078. PMID 8016118. Bibcode1994PNAS...91.6078P. 

External links