16S rRNA (adenine1408-N1)-methyltransferase

16S rRNA (adenine1408-N1)-methyltransferase
Identifiers
EC number 2.1.1.180
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 (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + adenine1408 in 16S rRNA S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA

The enzyme provides a panaminoglycoside resistance through interference with the binding of aminoglycosides.

References

  1. Beauclerk, A.A.; Cundliffe, E. (1987). "Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides". J. Mol. Biol. 193: 661–671. doi:10.1016/0022-2836(87)90349-4. PMID 2441068.
  2. Koscinski, L.; Feder, M.; Bujnicki, J.M. (2007). "Identification of a missing sequence and functionally important residues of 16S rRNA:m1A1408 methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics". Cell Cycle. 6: 1268–1271. doi:10.4161/cc.6.10.4231. PMID 17495534.
  3. Holmes, D.J.; Drocourt, D.; Tiraby, G.; Cundliffe, E. (1991). "Cloning of an aminoglycoside-resistance-encoding gene, kamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius". Gene. 102: 19–26. doi:10.1016/0378-1119(91)90532-g. PMID 1840536.
  4. Wachino, J.; Shibayama, K.; Kurokawa, H.; Kimura, K.; Yamane, K.; Suzuki, S.; Shibata, N.; Ike, Y.; Arakawa, Y. (2007). "Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides". Antimicrob. Agents Chemother. 51: 4401–4409. doi:10.1128/aac.00926-07. PMID 17875999.

External links

This article is issued from Wikipedia - version of the 5/16/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.