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S8/S53 domain
Structure of pseudomonalisin (PDB: 1GA6​)
Identifiers
Symbol	Peptidase_S8
Pfam	PF00082
InterPro	IPR000209
PROSITE	PDOC00125
CATH	1GA6
SCOP2	1GA6 / SCOPe / SUPFAM
CDD	cd07477
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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.

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.

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 -Glu-Ala-, -Leu-Tyr- and -Phe-Tyr-, and angiotensin I at -Tyr-Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-Phe(NO₂)-Arg-Leu.

Xanthomonalisin

Xanthomonalisin (Q60106) is found in Xanthomonas bacteria. It cleaves caesin and clots milk.

Physarolisin

Physarolisin (Q8MZS4, physaropepsin) is a milk-clotting enzyme. It shows preferential cleavage of Gly-Ser in B chain of insulin most rapidly, followed by Leu!Val, Cys(SO₃H)-Gly and Phe-Phe.

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.

References

1. "Family S53: Summary". MEROPS - the Peptidase Database.
2. Oda K (January 2012). "New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases". Journal of Biochemistry. 151 (1): 13–25. doi:10.1093/jb/mvr129. PMID 22016395.
3. Oda K, Sugitani M, Fukuhara K, Murao S (March 1987). "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. doi:10.1016/0304-4165(87)90055-9. PMID 3548827.
4. Oda K, Nakatani H, Dunn BM (April 1992). "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. doi:10.1016/0167-4838(92)90272-f. PMID 1562589.
5. Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, et al. (May 2001). "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes". Nature Structural Biology. 8 (5): 442–446. doi:10.1038/87610. PMID 11323721. S2CID 16793101.
6. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
7. Oda K, Nakazima T, Terashita T, Suzuki KI, Murao S (1987). "Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium". Agric. Biol. Chem. 51 (11): 3073–3080. doi:10.1271/bbb1961.51.3073.
8. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
9. Henney HR, Tavana G (1982). "Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum". Exp. Mycol. 6: 161–170. doi:10.1016/0147-5975(82)90090-1.
10. Murakami-Murofushi K, Hiratsuka A, Ohta J (1984). "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. doi:10.1247/csf.9.311.
11. North MJ, Whyte A (1984). "Purification and characterization of two acid proteinases from Dictyostelium discoideum". J. Gen. Microbiol. 130: 123–134. doi:10.1099/00221287-130-1-123.
12. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
13. Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N, et al. (February 2003). "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. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815.
14. Nishii W, Kuriyama H, Takahashi K (July 2003). "The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II". FEBS Letters. 546 (2–3): 340–344. doi:10.1016/S0014-5793(03)00621-5. PMID 12832065. S2CID 19197020.

External links

• Sedolisin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Physarolisin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Xanthomonalisin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.21