Biology:Sedolisin
| S8/S53 domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| Symbol | Peptidase_S8 | ||||||||
| Pfam | PF00082 | ||||||||
| InterPro | IPR000209 | ||||||||
| PROSITE | PDOC00125 | ||||||||
| CATH | 1GA6 | ||||||||
| SCOP2 | 1GA6 / SCOPe / SUPFAM | ||||||||
| CDD | cd07477 | ||||||||
| |||||||||
The sedolisin (MEROPS S53) family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.[1]
Their optimal pH is around 3. Most members of the family are produced as a precursor protein with N-terminal (InterPro: IPR015366) and sometimes C-terminal peptides that need to be cleaved off.[2]
Family members
Sedolisin
Sedolisin (P42790, pseudomonapepsin, sedolysin) is a serine protease. It is secreted by Pseudomonas sp. 101. It performs 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.[3][4][5][6]
Xanthomonalisin
| Xanthomonalisin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.101 | ||||||||
| CAS number | 113356-29-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Xanthomonalisin (Q60106) is found in Xanthomonas bacteria. It cleaves caesin and clots milk.[7][8]
Physarolisin
| Physarolisin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.103 | ||||||||
| CAS number | 94949-28-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Physarolisin (Q8MZS4, physaropepsin) is a milk-clotting enzyme. It shows preferential cleavage of Gly8-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-Gly and Phe24-Phe.[9][10][11][12][13]
It is special in that it is cold-adapted. It was discovered in the slime mold Physarum flavicomum. Similar proteins (InterPro: IPR017001) are also found in archaea.[14]
References
- ↑ "Family S53: Summary". https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S53.
- ↑ "New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases". Journal of Biochemistry 151 (1): 13–25. January 2012. doi:10.1093/jb/mvr129. PMID 22016395.
- ↑ "Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium". Biochimica et Biophysica Acta (BBA) - General Subjects 923 (3): 463–469. 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 (BBA) - Protein Structure and Molecular Enzymology 1120 (2): 208–214. 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): 442–446. 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. doi:10.18388/abp.2003_3716. PMID 12673349.
- ↑ "Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium". Agric. Biol. Chem. 51 (11): 3073–3080. 1987. doi:10.1271/bbb1961.51.3073.
- ↑ "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica 50 (1): 81–102. 2003. doi:10.18388/abp.2003_3716. PMID 12673349.
- ↑ "Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum". Exp. Mycol. 6: 161–170. 1982. doi:10.1016/0147-5975(82)90090-1.
- ↑ "A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia". Cell Struct. Funct. 9 (3): 311–315. 1984. doi:10.1247/csf.9.311.
- ↑ "Purification and characterization of two acid proteinases from Dictyostelium discoideum". J. Gen. Microbiol. 130: 123–134. 1984. doi:10.1099/00221287-130-1-123.
- ↑ "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica 50 (1): 81–102. 2003. doi:10.18388/abp.2003_3716. PMID 12673349.
- ↑ "Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase". Biochemical and Biophysical Research Communications 301 (4): 1023–1029. February 2003. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815.
- ↑ "The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II". FEBS Letters 546 (2–3): 340–344. July 2003. doi:10.1016/S0014-5793(03)00621-5. PMID 12832065.
External links
- Sedolisin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Physarolisin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Xanthomonalisin at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
