TRNKHis guanililtransferaza
| TRNKHis guanililtransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.7.79 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
TRNKHis guanililtransferaza (EC 2.7.7.79, histidin tRNK guanililtransferaza, Thg1p, Thg1) je enzim sa sistematskim imenom p-tRNKHis:GTP guanililtransferaza (ATP-hidroliza).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- p-tRNKHis + ATP + GTP pppGp-tRNKHis + AMP + difosfat (sveukupna reakcija)
- (1a) p-tRNKHis + ATP App-tRNKHis + difosfat
- (1b) App-tRNKHis + GTP pppGp-tRNKHis + AMP
Kod eukariota jedan dodatni guanozinski ostatak je dodata posttranskripciono na 5'-kraj tRNKHis molekula.
Reference
[уреди | уреди извор]- ^ Jahn, D. & Pande, S. (1991). „Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism”. J. Biol. Chem. 266: 22832—22836. PMID 1660462.
- ^ Pande, S., Jahn, D. and Soll, D. (1991). „Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties”. J. Biol. Chem. 266: 22826—22831. PMID 1660461.
- ^ Gu, W., Jackman, J.E., Lohan, A.J., Gray, M.W. and Phizicky, E.M. (2003). „tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5′ end of tRNAHis”. Genes Dev. 17: 2889—2901. PMID 14633974.
- ^ Placido, A., Sieber, F., Gobert, A., Gallerani, R., Giege, P. and Marechal-Drouard, L. (2010). „Plant mitochondria use two pathways for the biogenesis of tRNAHis”. Nucleic Acids Res. 38: 7711—7717. PMID 20660484.
- ^ Jackman, J.E. & Phizicky, E.M. (2008). „Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase”. Biochemistry. 47: 4817—4825. PMID 18366186.
- ^ Hyde, S.J., Eckenroth, B.E., Smith, B.A., Eberley, W.A., Heintz, N.H., Jackman, J.E. and Doublie, S. (2010). „tRNA(His) guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases”. Proc. Natl. Acad. Sci. USA. 107: 20305—20310. PMID 21059936.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- TRNAHis+guanylyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)
