Biology:16S rRNA (guanine1405-N7)-methyltransferase
From HandWiki
Short description: Class of enzymes
| 16S rRNA (guanine1405-N7)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.179 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
16S 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 reaction
- S-adenosyl-L-methionine + guanine1405 in 16S rRNA [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
The enzyme specifically methylates guanine1405 at N7 in 16S rRNA.
References
- ↑ "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): 4120–32. July 2010. doi:10.1093/nar/gkq122. PMID 20194115.
- ↑ "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): 5420–31. September 2009. doi:10.1093/nar/gkp575. PMID 19589804.
- ↑ "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 (9–10): 658–62. 2008. doi:10.1016/j.resmic.2008.09.006. PMID 18930134.
- ↑ "Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm". Journal of Bacteriology 190 (17): 5855–61. September 2008. doi:10.1128/jb.00076-08. PMID 18586937.
- ↑ "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): 582–90. April 2008. doi:10.1016/j.bbapap.2007.09.009. PMID 18343347.
- ↑ "Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis". Journal of Bacteriology 174 (23): 7868–72. December 1992. doi:10.1128/jb.174.23.7868-7872.1992. PMID 1447159.
- ↑ "Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases". Journal of Molecular Biology 388 (3): 570–82. May 2009. doi:10.1016/j.jmb.2009.03.034. PMID 19303884.
- ↑ "RmtC introduces G1405 methylation in 16S rRNA and confers high-level aminoglycoside resistance on Gram-positive microorganisms". FEMS Microbiology Letters 311 (1): 56–60. October 2010. doi:10.1111/j.1574-6968.2010.02068.x. PMID 20722735.
- ↑ "Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens". Journal of Molecular Biology 359 (2): 358–64. June 2006. doi:10.1016/j.jmb.2006.03.038. PMID 16626740.
External links
- 16S+rRNA+(guanine1405-N7)-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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