TRNAHis guanylyltransferase
TRNAHis guanylyltransferase (EC 2.7.7.79, histidine tRNA guanylyltransferase, Thg1p, Thg1) is an enzyme with systematic name p-tRNAHis:GTP guanylyltransferase (ATP-hydrolysing).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate (overall reaction)
- (1a) p-tRNAHis + ATP
App-tRNAHis + diphosphate
- (1b) App-tRNAHis + GTP
pppGp-tRNAHis + AMP
The enzyme requires a divalent cation for activity.
References
- ↑ Jahn, D. and Pande, S. (1991). "Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism". J. Biol. Chem. 266 (34): 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 (34): 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 (23): 2889–2901. doi:10.1101/gad.1148603. 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 (21): 7711–7717. doi:10.1093/nar/gkq646. 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 (16): 4817–4825. doi:10.1021/bi702517q. 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 (47): 20305–20310. doi:10.1073/pnas.1010436107. PMID 21059936.
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