Sedolisin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.100 sedolisin
Sedolisin is an aspartic-peptidase-like serine-carboxyl peptidase secreted by Pseudomonas sp. No. 101, optimum pH 4, distinguished from xanthomonapepsin by insensitivity to EPNP and from scytalidopepsin B by this property and unrelated sequence, inhibited by the peptide aldehyde tyrostatin and the type example of family S53; it hydrolyses the insulin B chain at Glu13-Ala, Leu15-Tyr and Phe25-Tyr and angiotensin I at Tyr4-Ile, with Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Leu as a good synthetic substrate. By digesting proteins at acidic pH it supports bacterial acid-dependent proteolysis. It is distributed across Eukaryota and Bacteria.
Sedolisin is an aspartic-peptidase-like serine-carboxyl peptidase secreted by Pseudomonas sp. No. 101, optimum pH 4, distinguished from xanthomonapepsin by insensitivity to EPNP and from scytalidopepsin B by this property and unrelated sequence, inhibited by the peptide aldehyde tyrostatin and the type example of family S53; it hydrolyses the insulin B chain at Glu13-Ala, Leu15-Tyr and Phe25-Tyr and angiotensin I at Tyr4-Ile, with Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Leu as a good synthetic substrate. By digesting proteins at acidic pH it supports bacterial acid-dependent proteolysis. It is distributed across Eukaryota and Bacteria.
References:
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