[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/16s-rrna-guanine1405-n7-methyltransferase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/16s-rrna-guanine1405-n7-methyltransferase-wikipedia\/","headline":"16S rRNA (guanine1405-N7)-methyltransferase – Wikipedia","name":"16S rRNA (guanine1405-N7)-methyltransferase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 16S rRNA (guanine1405-N7)-methyltransferase (EC 2.1.1.179, methyltransferase Sgm, m7G1405 Mtase, Sgm Mtase, Sgm, sisomicin-gentamicin","datePublished":"2018-10-12","dateModified":"2018-10-12","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\/16s-rrna-guanine1405-n7-methyltransferase-wikipedia\/","about":["Wiki"],"wordCount":2770,"articleBody":" (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia (adsbygoogle = window.adsbygoogle || []).push({});after-content-x416S rRNA (guanine1405-N7)-methyltransferase (EC 2.1.1.179, methyltransferase Sgm, m7G1405 Mtase, Sgm Mtase, Sgm, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin methylase, GrmA, RmtB, RmtC, ArmA) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-methyltransferase.[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reactionS-adenosyl-L-methionine + guanine1405 in 16S rRNA (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4\u21cc{displaystyle rightleftharpoons } S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNAThe enzyme specifically methylates guanine1405 at N7 in 16S rRNA.References[edit]^ Husain N, Tkaczuk KL, Tulsidas SR, Kaminska KH, Cubrilo S, Maravi\u0107-Vlahovicek G, Bujnicki JM, Sivaraman J (July 2010). “Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases”. Nucleic Acids Research. 38 (12): 4120\u201332. doi:10.1093\/nar\/gkq122. PMC\u00a02896518. PMID\u00a020194115.^ Savic M, Lovric J, Tomic TI, Vasiljevic B, Conn GL (September 2009). “Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics”. Nucleic Acids Research. 37 (16): 5420\u201331. doi:10.1093\/nar\/gkp575. PMC\u00a02760815. PMID\u00a019589804.^ Tomic TI, Moric I, Conn GL, Vasiljevic B (2008). “Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site”. Research in Microbiology. 159 (9\u201310): 658\u201362. doi:10.1016\/j.resmic.2008.09.006. PMC\u00a02791848. PMID\u00a018930134.^ Savic M, Ilic-Tomic T, Macmaster R, Vasiljevic B, Conn GL (September 2008). “Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm”. Journal of Bacteriology. 190 (17): 5855\u201361. doi:10.1128\/jb.00076-08. PMC\u00a02519519. PMID\u00a018586937.^ Maravi\u0107 Vlahovicek G, Cubrilo S, Tkaczuk KL, Bujnicki JM (April 2008). “Modeling and experimental analyses reveal a two-domain structure and amino acids important for the activity of aminoglycoside resistance methyltransferase Sgm”. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics. 1784 (4): 582\u201390. doi:10.1016\/j.bbapap.2007.09.009. PMID\u00a018343347.^ Kojic M, Topisirovic L, Vasiljevic B (December 1992). “Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis”. Journal of Bacteriology. 174 (23): 7868\u201372. doi:10.1128\/jb.174.23.7868-7872.1992. PMC\u00a0207509. PMID\u00a01447159.^ Schmitt E, Galimand M, Panvert M, Courvalin P, Mechulam Y (May 2009). “Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases”. Journal of Molecular Biology. 388 (3): 570\u201382. doi:10.1016\/j.jmb.2009.03.034. PMID\u00a019303884.^ Wachino J, Shibayama K, Kimura K, Yamane K, Suzuki S, Arakawa Y (October 2010). “RmtC introduces G1405 methylation in 16S rRNA and confers high-level aminoglycoside resistance on Gram-positive microorganisms”. FEMS Microbiology Letters. 311 (1): 56\u201360. doi:10.1111\/j.1574-6968.2010.02068.x. PMID\u00a020722735.^ Liou GF, Yoshizawa S, Courvalin P, Galimand M (June 2006). “Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens”. Journal of Molecular Biology. 359 (2): 358\u201364. doi:10.1016\/j.jmb.2006.03.038. PMID\u00a016626740.External links[edit] (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\/16s-rrna-guanine1405-n7-methyltransferase-wikipedia\/#breadcrumbitem","name":"16S rRNA (guanine1405-N7)-methyltransferase – Wikipedia"}}]}]