Sedolisin Explained

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 and sometimes C-terminal peptides that need to be cleaved off.^[2]

Family members

Sedolisin

Sedolisin
Ec Number:	3.4.21.100
Cas Number:	848318-58-1

Sedolisin (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
Ec Number:	3.4.21.101
Cas Number:	113356-29-9

Xanthomonalisin is found in Xanthomonas bacteria. It cleaves caesin and clots milk.^{[7] [8]}

Physarolisin

Physarolisin
Ec Number:	3.4.21.103
Cas Number:	94949-28-7

Physarolisin (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 are also found in archaea.^[14]

Notes and References

1. Web site: Family S53: Summary . MEROPS - the Peptidase Database.
2. Oda K . New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases . Journal of Biochemistry . 151 . 1 . 13–25 . January 2012 . 22016395 . 10.1093/jb/mvr129 . free .
3. Oda K, Sugitani M, Fukuhara K, Murao S . 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 . 3548827 . 10.1016/0304-4165(87)90055-9 .
4. Oda K, Nakatani H, Dunn BM . 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 . 1562589 . 10.1016/0167-4838(92)90272-f .
5. Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K . 6 . Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes . Nature Structural Biology . 8 . 5 . 442–446 . May 2001 . 11323721 . 10.1038/87610 . 16793101 .
6. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K . Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases . Acta Biochimica Polonica . 50 . 1 . 81–102 . 2003 . 12673349 . 10.18388/abp.2003_3716 . free .
7. Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium . Oda K, Nakazima T, Terashita T, Suzuki KI, Murao S . Agric. Biol. Chem. . 1987 . 51 . 11 . 3073–3080 . 10.1271/bbb1961.51.3073. free .
8. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K . Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases . Acta Biochimica Polonica . 50 . 1 . 81–102 . 2003 . 12673349 . 10.18388/abp.2003_3716 . free .
9. Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum . Henney HR, Tavana G . Exp. Mycol. . 1982 . 6 . 161–170 . 10.1016/0147-5975(82)90090-1.
10. A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia . Murakami-Murofushi K, Hiratsuka A, Ohta J . Cell Struct. Funct. . 1984 . 9 . 3 . 311–315 . 10.1247/csf.9.311. free .
11. Purification and characterization of two acid proteinases from Dictyostelium discoideum . North MJ, Whyte A . J. Gen. Microbiol. . 1984 . 130 . 123–134 . 10.1099/00221287-130-1-123. free .
12. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K . Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases . Acta Biochimica Polonica . 50 . 1 . 81–102 . 2003 . 12673349 . 10.18388/abp.2003_3716 . free .
13. Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N, Murakami-Murofushi K, Takahashi K . 6 . 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 . 12589815 . 10.1016/s0006-291x(03)00083-4 .
14. Nishii W, Kuriyama H, Takahashi K . The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II . FEBS Letters . 546 . 2–3 . 340–344 . July 2003 . 12832065 . 10.1016/S0014-5793(03)00621-5 . 19197020 .