16S rRNK (adenin1408-N1)-metiltransferaza
(Preusmjereno sa stranice S-adenozil-L-metionin:16S rRNA (adenine1408-N1)-methyltransferase)
16S rRNK (adenin1408-N1 (EC 2.1.1.180, metilaza kanamicin-apramicinske otpornosti, 16S rRNK:m1A1408 metiltransferaza, KamB, NpmA, 16S rRNK m1A1408 metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:16S rRNK (adenin1408-N1)-metiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 16S rRNK (adenin1408-N1)-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.180 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- S-adenozil-L-metionin + adenin1408 u 16S rRNK S-adenozil-L-homocistein + N1-metiladenin1408 u 16S rRNK
Ovaj enzim pruža otpornost na panaminoglikozid ometanjem vezivanja aminoglikozida za A mesto 16S rRNK, tako što N1-metiliše u poziciji adenin1408.
Reference
uredi- ↑ Beauclerk, A.A. and Cundliffe, E. (1987). „Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides”. J. Mol. Biol. 193: 661-671. PMID 2441068.
- ↑ Koscinski, L., Feder, M. and 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. PMID 17495534.
- ↑ Holmes, D.J., Drocourt, D., Tiraby, G. and Cundliffe, E. (1991). „Cloning of an aminoglycoside-resistance-encoding gene, kamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius”. Gene 102: 19-26. PMID 1840536.
- ↑ Wachino, J., Shibayama, K., Kurokawa, H., Kimura, K., Yamane, K., Suzuki, S., Shibata, N., Ike, Y. and 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. PMID 17875999.
Literatura
uredi- 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.