[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/anthranilate-synthase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/anthranilate-synthase-wikipedia\/","headline":"Anthranilate synthase – Wikipedia","name":"Anthranilate synthase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 The enzyme anthranilate synthase (EC 4.1.3.27) catalyzes the chemical reaction chorismate + L-glutamine","datePublished":"2019-06-06","dateModified":"2019-06-06","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:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/anthranilate-synthase-wikipedia\/","wordCount":2540,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The enzyme anthranilate synthase (EC 4.1.3.27) catalyzes the chemical reactionchorismate + L-glutamine        (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4\u21cc{displaystyle rightleftharpoons } anthranilate + pyruvate + L-glutamateTable of ContentsFunction[edit]Reaction[edit]Structure and assembly[edit]Homologs[edit]Paralogs[edit]Nomenclature[edit]Structural studies[edit]Application[edit]References[edit]Function[edit]Anthranilate synthase creates anthranilate, an important intermediate in the biosynthesis of indole, and by extension, the amino acid tryptophan. Tryptophan can then be metabolized further into serotonin, melatonin, or various auxins.Reaction[edit]Anthranilate synthase catalyzes the change from chorismate to anthranilate. As its other substrate, it can use either glutamine or ammonia.[1] During the reaction, both a hydroxyl group and an enolpyruvyl group are removed from the aromatic ring. The enolpyruvyl group gains a proton to form pyruvate. It has been shown that the proton comes from the surrounding water and not from an intramolecular shift of a hydrogen atom on the substrates.[1] The amino group of glutamine (or ammonia itself) attacks chorismate in position 2, which leads to[how?] the elimination of enolpyruvyl group from position 3. In the process, an aromatic ring is re-formed.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4  Chemical equation of reaction occurring in anthranilate synthaseStructure and assembly[edit]The complex is made up of \u03b1 and \u03b2 subunits. Gel filtration experiments reveal that the complex occurs as an \u03b12\u03b22 tetramer under native conditions, and as an \u03b1\u03b2 dimer under high salt concentrations.[2] The \u03b1\u03b2 dimers interact through the \u03b1 subunits to form the complex.The subunits of anthranilate synthase are encoded by the trpE and trpD genes in E. coli, both of which appear in the trp operon.In Enterobacteriaceae, this enzyme exists in the form of an aggregate with anthranilate phosphoribosyltransferase. If these two enzymes are not clustered, the complex is unable to use glutamine as a substrate and can only use ammonia.[1]Homologs[edit]This section is empty.  You can help by adding to it.  (November 2013)Paralogs[edit]This section is empty.  You can help by adding to it.  (November 2013)Nomenclature[edit]This enzyme belongs to the family of lyases, to be specific the oxo-acid-lyases, which cleave carbon-carbon bonds.  The systematic name of this enzyme class is chorismate pyruvate-lyase (amino-accepting; anthranilate-forming). Other names in common use include anthranilate synthetase, chorismate lyase, and chorismate pyruvate-lyase (amino-accepting).  This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system – general.Structural studies[edit]As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes 1I1Q, 1I7Q, 1I7S, 1QDL, and 2I6Y.Application[edit]This section is empty.  You can help by adding to it.  (November 2013)References[edit]Baker TI, Crawford IP (1966). “Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli“. J. Biol. Chem. 241 (23): 5577\u20135584. doi:10.1016\/S0021-9258(18)96383-0. PMID\u00a05333199.Creighton TE, Yanofsky C (1970). “Chorismate to tryptophan (Escherichia coli) – Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase”. Methods Enzymol. 17A: 365\u2013380. doi:10.1016\/0076-6879(71)17215-1.Kung CC, Huang WN, Huang YC, Yeh KC (2006). “Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry”. Proteomics. 6 (9): 2746\u20132758. doi:10.1002\/pmic.200500108. PMID\u00a016526091. S2CID\u00a025896917.Ito J, Yanofsky C (1969). “Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits”. J. Bacteriol. 97 (2): 734\u2013742. doi:10.1128\/JB.97.2.734-742.1969. PMC\u00a0249753. PMID\u00a04886290.Zalkin H, Kling D (1968). “Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium“. Biochemistry. 7 (10): 3566\u20133573. doi:10.1021\/bi00850a034. PMID\u00a04878701.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.      (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/anthranilate-synthase-wikipedia\/#breadcrumbitem","name":"Anthranilate synthase – Wikipedia"}}]}]