EC 3.4.21.100

Reaction: Hydrolysis of the B chain of insulin at -Glu¹³Ala-, -Leu¹⁵Tyr- and -Phe²⁵Tyr-, and angiotensin I at -Tyr⁴Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-PhePhe(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, MEROPS, Metacyc, PDB, CAS registry number: 848318-58-1

References:

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]