[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/clavaminate-synthase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/clavaminate-synthase-wikipedia\/","headline":"Clavaminate synthase – Wikipedia","name":"Clavaminate synthase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme","datePublished":"2018-05-16","dateModified":"2018-05-16","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\/clavaminate-synthase-wikipedia\/","wordCount":2710,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating).[1][2][3][4][5] This enzyme catalyses the following chemical reaction(1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4\u21cc{displaystyle rightleftharpoons } amidinoproclavaminate + succinate + CO2(2) proclavaminate + 2-oxoglutarate + O2\u21cc{displaystyle rightleftharpoons } dihydroclavaminate + succinate + CO2 + H2O(3) dihydroclavaminate + 2-oxoglutarate + O2\u21cc{displaystyle rightleftharpoons } clavaminate + succinate + CO2 + H2OClavaminate synthase contains nonheme iron.References[edit]^ Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA (February 1991). “Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction”. Biochemistry. 30 (8): 2281\u201392. doi:10.1021\/bi00222a034. PMID\u00a01998687.^ Zhou, J.; Gunsior, M.; Bachmann, B.O.; Townsend, C.A.; Solomon, E.I. (1998). “Substrate binding to the \u03b1-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation”. J. Am. Chem. Soc. 120: 13539\u201313540. doi:10.1021\/ja983534x.^ Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ (February 2000). “Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase”. Nature Structural Biology. 7 (2): 127\u201333. doi:10.1038\/72398. PMID\u00a010655615.^ Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI (August 2001). “Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities”. Journal of the American Chemical Society. 123 (30): 7388\u201398. doi:10.1021\/ja004025+. PMID\u00a011472170.^ Townsend CA (October 2002). “New reactions in clavulanic acid biosynthesis”. Current Opinion in Chemical Biology. 6 (5): 583\u20139. doi:10.1016\/S1367-5931(02)00392-7. 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