2'-Fosfotransferaza
(Preusmjereno sa stranice Tpt1p)
2'-fosfotransferaza (EC 2.7.1.160, kvaščana 2'-fosfotransferaza, Tpt1, Tpt1p, 2'-fosfo-tRNK:NAD+ fosfotransferaza) je enzim sa sistematskim imenom 2'-fosfo-(ligirana tRNK):NAD+ fosfotransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 2'-fosfotransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.1.160 | ||||||||
| CAS broj | 126905-00-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 2'-fosfo-[tRNK] + NAD+ tRNK + ADP-riboza 1,2-fosfat + nikotinamid +H2O
Ovaj enzim katalizuje finalni korak tRNK splajsovanja u kvascu Saccharomyces cerevisiae.
Reference uredi
- ↑ Steiger, M.A., Kierzek, R., Turner, D.H. and Phizicky, E.M. (2001). „Substrate recognition by a yeast 2′-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog”. Biochemistry 40: 14098-14105. PMID 11705403.
- ↑ Spinelli, S.L., Kierzek, R., Turner, D.H. and Phizicky, E.M. (1999). „Transient ADP-ribosylation of a 2′-phosphate implicated in its removal from ligated tRNA during splicing in yeast”. J. Biol. Chem. 274: 2637-2644. PMID 9915792.
- ↑ Culver, G.M., McCraith, S.M., Consaul, S.A., Stanford, D.R. and Phizicky, E.M. (1997). „A 2′-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae”. J. Biol. Chem. 272: 13203-13210. PMID 9148937.
- ↑ McCraith, S.M. and Phizicky, E.M. (1991). „An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2′-phosphate from ligated tRNA to an acceptor molecule”. J. Biol. Chem. 266: 11986-11992. PMID 2050693.
- ↑ Hu, Q.D., Lu, H., Huo, K., Ying, K., Li, J., Xie, Y., Mao, Y. and Li, Y.Y. (2003). „A human homolog of the yeast gene encoding tRNA 2′-phosphotransferase: cloning, characterization and complementation analysis”. Cell. Mol. Life Sci. 60: 1725-1732. PMID 14504659.
- ↑ Steiger, M.A., Jackman, J.E. and Phizicky, E.M. (2005). „Analysis of 2′-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism”. RNA 11: 99-106. PMID 15611300.
- ↑ Sawaya, R., Schwer, B. and Shuman, S. (2005). „Structure-function analysis of the yeast NAD+-dependent tRNA 2′-phosphotransferase Tpt1”. RNA 11: 107-113. PMID 15611301.
- ↑ Kato-Murayama, M., Bessho, Y., Shirouzu, M. and Yokoyama, S. (2005). „Crystal structure of the RNA 2′-phosphotransferase from Aeropyrum pernix K1”. J. Mol. Biol. 348: 295-305. PMID 15811369.
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.