[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/sedolisin-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/sedolisin-wikipedia\/","headline":"Sedolisin – Wikipedia","name":"Sedolisin – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 The sedolisin (MEROPS S53) family of peptidases are a family of serine proteases","datePublished":"2020-02-09","dateModified":"2020-02-09","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","height":"101","width":"135"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/sedolisin-wikipedia\/","wordCount":3709,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The 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:\u00a0IPR015366) and sometimes C-terminal peptides that need to be cleaved off.[2]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFamily members[edit]Sedolisin[edit]Xanthomonalisin[edit]Physarolisin[edit]References[edit]External links[edit]Family members[edit]Sedolisin[edit]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[edit]Xanthomonalisin (Q60106) is found in Xanthomonas bacteria. It cleaves caesin and clots milk.[7][8]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Physarolisin[edit]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:\u00a0IPR017001) are also found in archaea.[14]References[edit]^ “Family S53: Summary”. MEROPS – the Peptidase Database.^ Oda K (January 2012). “New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases”. Journal of Biochemistry. 151 (1): 13\u201325. doi:10.1093\/jb\/mvr129. PMID\u00a022016395.^ 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\u2013469. doi:10.1016\/0304-4165(87)90055-9. PMID\u00a03548827.^ 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\u2013214. doi:10.1016\/0167-4838(92)90272-f. PMID\u00a01562589.^ Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H,  et\u00a0al. (May 2001). “Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes”. Nature Structural Biology. 8 (5): 442\u2013446. doi:10.1038\/87610. PMID\u00a011323721. S2CID\u00a016793101.^ 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\u2013102. doi:10.18388\/abp.2003_3716. PMID\u00a012673349.^ 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\u20133080. doi:10.1271\/bbb1961.51.3073.^ 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\u2013102. doi:10.18388\/abp.2003_3716. PMID\u00a012673349.^ 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\u2013170. doi:10.1016\/0147-5975(82)90090-1.^ 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\u2013315. doi:10.1247\/csf.9.311.^ North MJ, Whyte A (1984). “Purification and characterization of two acid proteinases from Dictyostelium discoideum“. J. Gen. Microbiol. 130: 123\u2013134. doi:10.1099\/00221287-130-1-123.^ 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\u2013102. doi:10.18388\/abp.2003_3716. PMID\u00a012673349.^ Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N,  et\u00a0al. (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\u20131029. doi:10.1016\/s0006-291x(03)00083-4. PMID\u00a012589815.^ 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\u20133): 340\u2013344. doi:10.1016\/S0014-5793(03)00621-5. PMID\u00a012832065. S2CID\u00a019197020.External links[edit]Wikimedia ErrorOur servers are currently under maintenance or experiencing a technical problem.Please try again in a few\u00a0minutes.See the error message at the bottom of this page for more\u00a0information.      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