23S rRNK (adenin2503-C2)-metiltransferaza
23S rRNK (adenin2503-C2)-metiltransferaza (EC 2.1.1.192, RlmN, YfgB, Cfr) je enzim sa sistematskim imenom S-adenozil-L-metionin:23S rRNK (adenin2503-C2)-metiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 23S rRNK (adenin2503-C2)-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.192 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 2 S-adenozil-L-metionin + adenin2503 u 23S rRNK S-adenozil-L-homocistein + L-metionin + 5'-dezoksiadenozin + 2-metiladenin2503 u 23S rRNK
Ovaj enzim sadrži [4Fe-4S] klaster. On je član familije AdoMet radikala (radikal SAM). S-adenozil-L-metionin deluje kao generator radikala i kao izvor metil grupa. RlmN je endogeni enzim koji ćelije koriste da rafiniraju funcionisanje ribozoma u proteinskoj sintezi. Enzim metiliše adenozin mehanizmom radikala sa CH2 sa S-adenozil-L-metionina i zadržavanjem vodonika u C-2 adenozina2503 na 23S rRNK. On takođe metiliše 8-metiladenozin2503 unutar 23S rRNK, cf. EC 2.1.1.224 [23-[S rRNK (adenin2503-C8)-metiltransferaza].
Reference
uredi- ↑ Toh, S.M., Xiong, L., Bae, T. and Mankin, A.S. (2008). „The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA”. RNA 14: 98-106. PMID 18025251.
- ↑ Yan, F., LaMarre, J.M., Röhrich, R., Wiesner, J., Jomaa, H., Mankin, A.S., Fujimori, D.G. (2010). „RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA”. J. Am. Chem. Soc. 132: 3953-3964. PMID 20184321.
- ↑ Yan, F. and Fujimori, D.G. (2011). „RNA methylation by Radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift”. Proc. Natl. Acad. Sci. USA 108: 3930-3934. PMID 21368151.
- ↑ Grove, T.L., Benner, J.S., Radle, M.I., Ahlum, J.H., Landgraf, B.J., Krebs, C. and Booker, S.J. (2011). „A radically different mechanism for S-adenosylmethionine-dependent methyltransferases”. Science 332: 604-607. PMID 21415317.
- ↑ Boal, A.K., Grove, T.L., McLaughlin, M.I., Yennawar, N.H., Booker, S.J. and Rosenzweig, A.C. (2011). „Structural basis for methyl transfer by a radical SAM enzyme”. Science 332: 544-545. PMID 21527678.
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.