Biology:Pseudomonalisin
From HandWiki
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
- ↑ "Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium". Biochimica et Biophysica Acta 923 (3): 463–9. March 1987. doi:10.1016/0304-4165(87)90055-9. PMID 3548827.
- ↑ "Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101". Biochimica et Biophysica Acta 1120 (2): 208–14. April 1992. doi:10.1016/0167-4838(92)90272-f. PMID 1562589.
- ↑ "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes". Nature Structural Biology 8 (5): 442–6. May 2001. doi:10.1038/87610. PMID 11323721.
- ↑ "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica 50 (1): 81–102. 2003. PMID 12673349. http://www.actabp.pl/pdf/1_2003/81.pdf.
External links
- Sedolisin at the US National Library of Medicine Medical Subject Headings (MeSH)
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