TRNKHis guanililtransferaza
Izgled
TRNKHis guanililtransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.7.79 | ||||||||
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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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.
- ↑ Jahn, D. and 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. and 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.
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