Pseudomonalisin
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
- ↑ Oda, K., Sugitani, M., Fukuhara, K. and 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.
- ↑ Oda, K., Nakatani, H. and 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.
- ↑ Wlodawer, A., Li, M., Dauter, Z., Gustchina, A., Uchida, K., Oyama, H., Dunn, B.M. and 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.
- ↑ Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M. and 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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