TRNA(His) guanylyltransferase
| tRNA(His) guanylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.79 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
tRNA(His) guanylyltransferase (EC 2.7.7.79, histidine tRNA guanylyltransferase, Thg1p, Thg1) is an enzyme with systematic name p-tRNA(His):GTP guanylyltransferase (ATP-hydrolysing).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- p-tRNA(His) + ATP + GTP pppGp-tRNA(His) + AMP + diphosphate (overall reaction)
- (1a) p-tRNA(His) + ATP App-tRNA(His) + diphosphate
- (1b) App-tRNA(His) + GTP pppGp-tRNA(His) + AMP
The enzyme requires a divalent cation for activity.
References
[edit]- ^ Jahn D, Pande S (December 1991). "Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism". The Journal of Biological Chemistry. 266 (34): 22832–6. doi:10.1016/S0021-9258(18)54429-X. PMID 1660462.
- ^ Pande S, Jahn D, Söll D (December 1991). "Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties". The Journal of Biological Chemistry. 266 (34): 22826–31. doi:10.1016/S0021-9258(18)54428-8. PMID 1660461.
- ^ Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM (December 2003). "tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis". Genes & Development. 17 (23): 2889–901. doi:10.1101/gad.1148603. PMC 289149. PMID 14633974.
- ^ Placido A, Sieber F, Gobert A, Gallerani R, Giegé P, Maréchal-Drouard L (November 2010). "Plant mitochondria use two pathways for the biogenesis of tRNAHis". Nucleic Acids Research. 38 (21): 7711–7. doi:10.1093/nar/gkq646. PMC 2995067. PMID 20660484.
- ^ Jackman JE, Phizicky EM (April 2008). "Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase". Biochemistry. 47 (16): 4817–25. doi:10.1021/bi702517q. PMID 18366186.
- ^ Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S (November 2010). "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases". Proceedings of the National Academy of Sciences of the United States of America. 107 (47): 20305–10. doi:10.1073/pnas.1010436107. PMC 2996709. PMID 21059936.
External links
[edit]- TRNA(His)+guanylyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
