TRNK (uracil-5-)-metiltransferaza
(Preusmjereno sa stranice TRNA(m5U54)methyltransferase)
TRNK (uracil-5-)-metiltransferaza (EC 2.1.1.35, transfer RNK uracil54 5-metiltransferaza, transfer RNK uracil54 metilaza, tRNK uracil54 5-metiltransferaza, m5U54-metiltransferaza, tRNK:m5U54-metiltransferaza, RUMT, TRMA, 5-metiluridin54 tRNK metiltransferaza, tRNK(uracil-54,C5)-metiltransferaza, Trm2, tRNK(m5U54)metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:tRNK (uracil54-C5)-metiltransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
| TRNK (uracil-5-)-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.35 | ||||||||
| CAS broj | 37257-02-6 | ||||||||
| 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 + uridin54 in tRNK S-adenozil-L-homocistein + 5-metiluridin54 in tRNK
Za razliku od ovog enzima, EC 2.1.1.74 (metilintetrahidrofolat-tRNK-(uracil54-C5)-metiltransferaze (FADH2-oksidacija)), koristi 5,10-metilintetrahidrofolat i FADH2 kao izvor atoma za metilaciju U54.
Reference uredi
- ↑ Björk, G.R. and Svensson, I. (1969). „Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae”. Eur. J. Biochem. 9: 207-215. PMID 4896260.
- ↑ Greenberg, R. and Dudock, B. (1980). „Isolation and characterization of m5U-methyltransferase from Escherichia coli”. J. Biol. Chem. 255: 8296-8302. PMID 6997293.
- ↑ Hurwitz, J., Gold, M. and Anders, M. (1964). „The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. 3. Purification of soluble ribonucleic acid-methylating enzymes”. J. Biol. Chem. 239: 3462-3473. PMID 14245404.
- ↑ Delk, A.S., Nagle, D.P., Jr. and Rabinowitz, J.C. (1980). „Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2”. J. Biol. Chem. 255: 4387-4390. PMID 6768721.
- ↑ Kealey, J.T., Gu, X. and Santi, D.V. (1994). „Enzymatic mechanism of tRNA (m5U54)methyltransferase”. Biochimie 76: 1133-1142. PMID 7748948.
- ↑ Gu, X., Ivanetich, K.M. and Santi, D.V. (1996). „Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase is not sequence specific”. Biochemistry 35: 11652-11659. PMID 8794745.
- ↑ Becker, H.F., Motorin, Y., Sissler, M., Florentz, C. and Grosjean, H. (1997). „Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the TΨ-loop of yeast tRNAs”. J. Mol. Biol. 274: 505-518. PMID 9417931.
- ↑ Walbott, H., Leulliot, N., Grosjean, H. and Golinelli-Pimpaneau, B. (2008). „The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity”. Nucleic Acids Res. 36: 4929-4940. PMID 18653523.
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.