Sedolisin#Sedolisin

{{Infobox enzyme

| Name = Sedolisin

| EC_number = 3.4.21.100

| CAS_number = 848318-58-1

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Sedolisin ({{UniProt|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.{{cite journal | vauthors = Oda K, Sugitani M, Fukuhara K, Murao S | title = Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium | journal = Biochimica et Biophysica Acta (BBA) - General Subjects | volume = 923 | issue = 3 | pages = 463–469 | date = March 1987 | pmid = 3548827 | doi = 10.1016/0304-4165(87)90055-9 }}{{cite journal | vauthors = Oda K, Nakatani H, Dunn BM | title = Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101 | journal = Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology | volume = 1120 | issue = 2 | pages = 208–214 | date = April 1992 | pmid = 1562589 | doi = 10.1016/0167-4838(92)90272-f }}{{cite journal | vauthors = Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K | display-authors = 6 | title = Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes | journal = Nature Structural Biology | volume = 8 | issue = 5 | pages = 442–446 | date = May 2001 | pmid = 11323721 | doi = 10.1038/87610 | s2cid = 16793101 }}{{cite journal | vauthors = Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K | title = Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases | journal = Acta Biochimica Polonica | volume = 50 | issue = 1 | pages = 81–102 | date = 2003 | pmid = 12673349 | doi = 10.18388/abp.2003_3716 | doi-access = free }}

{{Infobox enzyme

| Name = Xanthomonalisin

| EC_number = 3.4.21.101

| CAS_number = 113356-29-9

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Xanthomonalisin ({{UniProt|Q60106}}) is found in Xanthomonas bacteria. It cleaves caesin and clots milk.{{cite journal | title = Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium | vauthors = Oda K, Nakazima T, Terashita T, Suzuki KI, Murao S |journal = Agric. Biol. Chem. |date = 1987 |volume = 51 | issue = 11 |pages = 3073–3080 |doi=10.1271/bbb1961.51.3073|doi-access = free }}{{cite journal | vauthors = Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K | title = Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases | journal = Acta Biochimica Polonica | volume = 50 | issue = 1 | pages = 81–102 | date = 2003 | pmid = 12673349 | doi = 10.18388/abp.2003_3716 | doi-access = free }}

{{Infobox enzyme

| Name = Physarolisin

| EC_number = 3.4.21.103

| CAS_number = 94949-28-7

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Physarolisin ({{UniProt|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.{{cite journal | title = Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum | vauthors = Henney HR, Tavana G |journal = Exp. Mycol. |date = 1982 |volume = 6 |pages = 161–170 |doi=10.1016/0147-5975(82)90090-1}}{{cite journal | title = A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia | vauthors = Murakami-Murofushi K, Hiratsuka A, Ohta J |journal = Cell Struct. Funct. |date = 1984 |volume = 9 | issue = 3 |pages = 311–315 |doi=10.1247/csf.9.311|doi-access = free }}{{cite journal | title = Purification and characterization of two acid proteinases from Dictyostelium discoideum | vauthors = North MJ, Whyte A |journal = J. Gen. Microbiol. |date = 1984 |volume = 130 |pages = 123–134 |doi=10.1099/00221287-130-1-123|doi-access = free }}{{cite journal | vauthors = Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K | title = Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases | journal = Acta Biochimica Polonica | volume = 50 | issue = 1 | pages = 81–102 | date = 2003 | pmid = 12673349 | doi = 10.18388/abp.2003_3716 | doi-access = free }}{{cite journal | vauthors = Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N, Murakami-Murofushi K, Takahashi K | display-authors = 6 | title = Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase | journal = Biochemical and Biophysical Research Communications | volume = 301 | issue = 4 | pages = 1023–1029 | date = February 2003 | pmid = 12589815 | doi = 10.1016/s0006-291x(03)00083-4 }}

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.{{cite journal | vauthors = Nishii W, Kuriyama H, Takahashi K | title = The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II | journal = FEBS Letters | volume = 546 | issue = 2–3 | pages = 340–344 | date = July 2003 | pmid = 12832065 | doi = 10.1016/S0014-5793(03)00621-5 | s2cid = 19197020 }}

{{reflist}}

• {{MeshName|Sedolisin}}
• {{MeshName|Physarolisin}}
• {{MeshName|Xanthomonalisin}}

{{Serine endopeptidases}}

{{Enzymes}}

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Category:EC 3.4.21