23S rRNK (uracil1939-C5)-metiltransferaza
23S rRNK (uracil1939-C5)-metiltransferaza (EC 2.1.1.190, RumA, RNK uridinska metiltransferaza A, YgcA) je enzim sa sistematskim imenom S-adenozil-L-metionin:23S rRNK (uracil1939-C5)-metiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 23S rRNK (uracil1939-C5)-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.190 | ||||||||
| 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 + uracil1939 u 23S rRNK S-adenozil-L-homocistein + 5-metiluracil1939 u 23S rRNK
Ovaj enzim specifično metiliše uracil1939 u C5 poziciji 23S rRNK. Enzim sadrži [4Fe-4S] klaster koji je koordinisan sa četiri konzervisana cisteinska ostataka.
Reference uredi
- ↑ Agarwalla, S., Kealey, J.T., Santi, D.V. and Stroud, R.M. (2002). „Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli”. J. Biol. Chem. 277: 8835-8840. PMID 11779873.
- ↑ Lee, T.T., Agarwalla, S. and Stroud, R.M. (2004). „Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase”. Structure 12: 397-407. PMID 15016356.
- ↑ Madsen, C.T., Mengel-Jorgensen, J., Kirpekar, F. and Douthwaite, S. (2003). „Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry”. Nucleic Acids Res. 31: 4738-4746. PMID 12907714.
- ↑ Persaud, C., Lu, Y., Vila-Sanjurjo, A., Campbell, J.L., Finley, J. and O'Connor, M. (2010). „Mutagenesis of the modified bases, m5U1939 and Ψ2504, in Escherichia coli 23S rRNA”. Biochem. Biophys. Res. Commun. 392: 223-227. PMID 20067766.
- ↑ Agarwalla, S., Stroud, R.M. and Gaffney, B.J. (2004). „Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies”. J. Biol. Chem. 279: 34123-34129. PMID 15181002.
- ↑ Lee, T.T., Agarwalla, S. and Stroud, R.M. (2005). „A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function”. Cell 120: 599-611. PMID 15766524.
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.