16S rRNA (guanine1405-N7)-methyltransferase
From Wikipedia the free encyclopedia
| 16S rRNA (guanine1405-N7)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
The enzyme specifically methylates guanine1405 at N7 in 16S rRNA.
References[edit]
- ^ Husain N, Tkaczuk KL, Tulsidas SR, Kaminska KH, Cubrilo S, Maravić-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): 4120–32. doi:10.1093/nar/gkq122. PMC 2896518. PMID 20194115.
- ^ 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): 5420–31. doi:10.1093/nar/gkp575. PMC 2760815. PMID 19589804.
- ^ 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 (9–10): 658–62. doi:10.1016/j.resmic.2008.09.006. PMC 2791848. PMID 18930134.
- ^ 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): 5855–61. doi:10.1128/jb.00076-08. PMC 2519519. PMID 18586937.
- ^ Maravić 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): 582–90. doi:10.1016/j.bbapap.2007.09.009. PMID 18343347.
- ^ Kojic M, Topisirovic L, Vasiljevic B (December 1992). "Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis". Journal of Bacteriology. 174 (23): 7868–72. doi:10.1128/jb.174.23.7868-7872.1992. PMC 207509. PMID 1447159.
- ^ 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): 570–82. doi:10.1016/j.jmb.2009.03.034. PMID 19303884.
- ^ 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): 56–60. doi:10.1111/j.1574-6968.2010.02068.x. PMID 20722735.
- ^ 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): 358–64. doi:10.1016/j.jmb.2006.03.038. PMID 16626740.
External links[edit]
- 16S+rRNA+(guanine1405-N7)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
