16S rRNA (guanine1405-N7)-methyltransferase

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
Search PMC articles PubMed articles NCBI proteins

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 + guanine ¹⁴⁰⁵ in 16S rRNA ${\displaystyle \rightleftharpoons }$ S-adenosyl-L-homocysteine + 7-methylguanine ¹⁴⁰⁵ in 16S rRNA

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

References

1. 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.
2. 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.
3. 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.
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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

• 16S+rRNA+(guanine1405-N7)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)