16S rRNK (guanin1405-N7)-metiltransferaza
Prijeđi na navigaciju
Prijeđi na pretragu
| 16S rRNK (guanin1405-N7)-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.179 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
16S rRNK (guanin1405-N7)-metiltransferaza (EC 2.1.1.179, metiltransferaza Sgm, m7G1405 Mtaze, Sgm Mtaze, Sgm, sisomicin-gentamicinska metiltransferaza, sisomicin-gentamicinska metilaza, GrmA, RmtB, RmtC, ArmA) je enzim sa sistematskim imenom S-adenozil-L-metionin:16S rRNK (guanin1405-N7)-metiltransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- S-adenozil-L-metionin + guanin1405 u 16S rRNK S-adenozil-L-homocistein + 7-metilguanin1405 u 16S rRNK
Ovaj enzim specifično metiliše guanin1405 u N7 poziciji unutar 16S rRNK. Enzim iz bakterije Micromonospora zionensis, koja proizvodi antibiotike, metiliše guanin1405 u 16S rRNK do 7-metilguanina, što daje ribozomu otpornost na 4,6-disupstituisane dezoksistreptaminske aminoglikozide, kao što su gentamicini i kanamicini.
Reference[uredi | uredi kod]
- ↑ Husain, N., Tkaczuk, K.L., Tulsidas, S.R., Kaminska, K.H., Cubrilo, S., Maravic-Vlahovicek, G., Bujnicki, J.M. and 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. PMID 20194115.
- ↑ Savic, M., Lovric, J., Tomic, T.I., Vasiljevic, B. and 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. PMID 19589804.
- ↑ Tomic, T.I., Moric, I., Conn, G.L. and 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. PMID 18930134.
- ↑ Savic, M., Ilic-Tomic, T., Macmaster, R., Vasiljevic, B. and Conn, G.L. (2008). „Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm”. J. Bacteriol. 190: 5855-5861. PMID 18586937.
- ↑ Maravic Vlahovicek, G., Cubrilo, S., Tkaczuk, K.L. and 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. PMID 18343347.
- ↑ Kojic, M., Topisirovic, L. and Vasiljevic, B. (1992). „Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis”. J. Bacteriol. 174: 7868-7872. PMID 1447159.
- ↑ Schmitt, E., Galimand, M., Panvert, M., Courvalin, P. and Mechulam, Y. (2009). „Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases”. J. Mol. Biol. 388: 570-582. PMID 19303884.
- ↑ Wachino, J., Shibayama, K., Kimura, K., Yamane, K., Suzuki, S. and 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. PMID 20722735.
- ↑ Liou, G.F., Yoshizawa, S., Courvalin, P. and Galimand, M. (2006). „Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens”. J. Mol. Biol. 359: 358-364. PMID 16626740.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.