Metilentetrahidrofolat—tRNK-(uracil-5-)-metiltransferaza
(Preusmjereno sa stranice 5,10-methylenetetrahydrofolate:tRNA (uracil54-C5)-methyltransferase)
Metilentetrahidrofolat—tRNK-(uracil-5-)-metiltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.1.1.74 | ||||||||
CAS broj | 56831-74-4 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Metilentetrahidrofolat—tRNK-(uracil-5-)-metiltransferaza (EC 2.1.1.74, folat-zavisna ribotimidilna sintaza, metilintetrahidrofolatni-transfer ribonukleatni uracil 5-metiltransferaza, 5,10-metilintetrahidrofolat:tRNK-UPsiC (uracil-5-)-metil-transferaza, 5,10-metilintetrahidrofolat:tRNK (uracil-5-)-metil-transferaza, TrmFO, folat/FAD-zavisni tRNK T54 metiltransferaza) je enzim sa sistematskim imenom 5,10-metilintetrahidrofolat:tRNK (uracil54-C5)-metiltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5,10-metilintetrahidrofolat + uridin54 unutar tRNK + FADH2 tetrahidrofolat + 5-metiluridin54 unutar tRNK + FAD
Do 25% baza funkcionalne tRNK je posttranslaciono modifikovano ili hipermodifikovano. Jedna od skoro universalnih posttranslacionih modifikacija je konverzija U54 u ribotimidinu u TPsiC petlji.
- ↑ 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.
- ↑ 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.
- ↑ Nishimasu, H., Ishitani, R., Yamashita, K., Iwashita, C., Hirata, A., Hori, H. and Nureki, O. (2009). „Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase”. Proc. Natl. Acad. Sci. USA 106: 8180-8185. PMID 19416846.
- 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.