Pseudomonalisin

Sedolisin
Identifiers
EC number 3.4.21.100
CAS number 848318-58-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Sedolisin (EC 3.4.21.100, Pseudomonas sp. pepstatin-insensitive carboxyl proteinase, pseudomonapepsin, sedolysin) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of the B chain of insulin at -Glu13-Ala-, -Leu15-Tyr- and -Phe25-Tyr-, and angiotensin I at -Tyr4-Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Leu.

This enzyme is secreted by Pseudomonas sp. No. 101.

References

  1. ↑ Oda, K.; Sugitani, M.; Fukuhara, K.; Murao, S. (1987). "Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium". Biochim. Biophys. Acta. 923 (3): 463–469. doi:10.1016/0304-4165(87)90055-9. PMID 3548827.
  2. ↑ Oda, K.; Nakatani, H.; Dunn, B.M. (1992). "Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101". Biochim. Biophys. Acta. 1120 (2): 208–214. doi:10.1016/0167-4838(92)90272-f. PMID 1562589.
  3. ↑ Wlodawer, A.; Li, M.; Dauter, Z.; Gustchina, A.; Uchida, K.; Oyama, H.; Dunn, B.M.; Oda, K. (2001). "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes". Nat. Struct. Biol. 8 (5): 442–446. doi:10.1038/87610. PMID 11323721.
  4. ↑ Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Dunn, B.M.; Oda, K. (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochim. Pol. 50 (1): 81–102. PMID 12673349.
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