The Enzyme Database

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Accepted name: sedolisin
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.
Other name(s): Pseudomonas sp. pepstatin-insensitive carboxyl proteinase; pseudomonapepsin; pseudomonalisin; sedolysin
Comments: An enzyme secreted by Pseudomonas sp. No. 101. Optimum pH is 4. It is distinguished from xanthomonapepsin by its insensitivity to EPNP and from scytalidopepsin B by this property and by its unrelated amino-acid sequence. Inhibited by tyrostatin, a peptide aldehyde [2]. Type example of peptidase family S53.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 848318-58-1
1.  Oda, K., Sugitani, M., Fukuhara, K. and Murao, S. Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium. Biochim. Biophys. Acta 923 (1987) 463–469. [PMID: 3548827]
2.  Oda, K., Nakatani, H. and Dunn, B.M. Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101. Biochim. Biophys. Acta 1120 (1992) 208–214. [PMID: 1562589]
3.  Wlodawer, A., Li, M., Dauter, Z., Gustchina, A., Uchida, K., Oyama, H., Dunn, B.M. and Oda, K. Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes. Nat. Struct. Biol. 8 (2001) 442–446. [PMID: 11323721]
4.  Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M. and Oda, K. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Acta Biochim. Pol. 50 (2003) 81–102. [PMID: 12673349]
[EC created 1995 as EC, transferred 2001 to EC, modified 2003]

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