|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions|
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 16S rRNA (guanine1405-N7)-methyltransferase
Enzyme Commission Synonyms: methyltransferase Sgm, m7G1405 Mtase, Sgm Mtase, Sgm, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin methylase, GrmA, RmtB, RmtC, ArmA
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -24.765076 [Latendresse13]
Enzyme Commission Summary:
The enzyme specifically methylates guanine1405 at C7 in 16S rRNA. The enzyme from the antibiotic-producing bacterium Micromonospora zionensis methylates guanine1405 in 16S rRNA to 7-methylguanine, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins [Savic09].
Husain10a: Husain N, Tkaczuk KL, Tulsidas SR, Kaminska KH, Cubrilo S, Maravic-Vlahovicek G, Bujnicki JM, 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(12);4120-32. PMID: 20194115
Kojic92: Kojic M, Topisirovic L, Vasiljevic B (1992). "Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis." J Bacteriol 174(23);7868-72. PMID: 1447159
Liou06: Liou GF, Yoshizawa S, Courvalin P, Galimand M (2006). "Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens." J Mol Biol 359(2);358-64. PMID: 16626740
Maravic08: Maravic Vlahovicek G, Cubrilo S, Tkaczuk KL, Bujnicki JM (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(4);582-90. PMID: 18343347
Savic08: Savic M, Ilic-Tomic T, Macmaster R, Vasiljevic B, Conn GL (2008). "Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm." J Bacteriol 190(17);5855-61. PMID: 18586937
Savic09: Savic M, Lovric J, Tomic TI, Vasiljevic B, Conn GL (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(16);5420-31. PMID: 19589804
Schmitt09: 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(3);570-82. PMID: 19303884
Tomic: Tomic TI, Moric I, Conn GL, Vasiljevic B "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(9-10);658-62. PMID: 18930134
Wachino10: 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(1);56-60. PMID: 20722735
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493