16S rRNA (guanine1405-N7)-methyltransferase

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 S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA

The enzyme specifically methylates guanine1405 at N7 in 16S rRNA.

References

  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. 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. 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. 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. 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. 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.

External links

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