16S rRNA (guanine1405-N7)-methyltransferase

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16S rRNA (guanine1405-N7)-methyltransferase
EC number
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MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

16S rRNA (guanine1405-N7)-methyltransferase (EC, 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.


  1. ^ Husain, N.; Tkaczuk, K.L.; Tulsidas, S.R.; Kaminska, K.H.; Cubrilo, S.; Maravic-Vlahovicek, G.; Bujnicki, J.M.; Sivaraman, J. (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 Res. 38: 4120–4132. doi:10.1093/nar/gkq122. PMC 2896518Freely accessible. PMID 20194115. 
  2. ^ Savic, M.; Lovric, J.; Tomic, T.I.; Vasiljevic, B.; Conn, G.L. (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 Res. 37: 5420–5431. doi:10.1093/nar/gkp575. PMC 2760815Freely accessible. PMID 19589804. 
  3. ^ Tomic, T.I.; Moric, I.; Conn, G.L.; 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". Res. Microbiol. 159: 658–662. doi:10.1016/j.resmic.2008.09.006. PMC 2791848Freely accessible. PMID 18930134. 
  4. ^ Savic, M.; Ilic-Tomic, T.; Macmaster, R.; Vasiljevic, B.; Conn, G.L. (2008). "Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm". J. Bacteriol. 190: 5855–5861. doi:10.1128/jb.00076-08. PMC 2519519Freely accessible. PMID 18586937. 
  5. ^ Maravic Vlahovicek, G.; Cubrilo, S.; Tkaczuk, K.L.; Bujnicki, J.M. (2008). "Modeling and experimental analyses reveal a two-domain structure and amino acids important for the activity of aminoglycoside resistance methyltransferase Sgm". Biochim. Biophys. Acta. 1784: 582–590. doi:10.1016/j.bbapap.2007.09.009. PMID 18343347. 
  6. ^ Kojic, M.; Topisirovic, L.; Vasiljevic, B. (1992). "Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis". J. Bacteriol. 174: 7868–7872. PMC 207509Freely accessible. PMID 1447159. 
  7. ^ Schmitt, E.; Galimand, M.; Panvert, M.; Courvalin, P.; Mechulam, Y. (2009). "Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases". J. Mol. Biol. 388: 570–582. doi:10.1016/j.jmb.2009.03.034. PMID 19303884. 
  8. ^ Wachino, J.; Shibayama, K.; Kimura, K.; Yamane, K.; Suzuki, S.; Arakawa, Y. (2010). "RmtC introduces G1405 methylation in 16S rRNA and confers high-level aminoglycoside resistance on Gram-positive microorganisms". FEMS Microbiol. Lett. 311: 56–60. doi:10.1111/j.1574-6968.2010.02068.x. PMID 20722735. 
  9. ^ Liou, G.F.; Yoshizawa, S.; Courvalin, P.; Galimand, M. (2006). "Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens". J. Mol. Biol. 359: 358–364. doi:10.1016/j.jmb.2006.03.038. PMID 16626740. 

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