词条 | TRNAHis guanylyltransferase |
释义 |
| Name = TRNAHis guanylyltransferase | EC_number = 2.7.7.79 | CAS_number = | IUBMB_EC_number = 2/7/7/79 | GO_code = | image = | width = | caption = }}TRNAHis guanylyltransferase ({{EC number|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. References1. ^{{cite journal | vauthors = Jahn D, Pande S | title = Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism | journal = The Journal of Biological Chemistry | volume = 266 | issue = 34 | pages = 22832–6 | date = December 1991 | pmid = 1660462 }} 2. ^{{cite journal | vauthors = Pande S, Jahn D, Söll D | title = Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties | journal = The Journal of Biological Chemistry | volume = 266 | issue = 34 | pages = 22826–31 | date = December 1991 | pmid = 1660461 }} 3. ^{{cite journal | vauthors = Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM | title = tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis | journal = Genes & Development | volume = 17 | issue = 23 | pages = 2889–901 | date = December 2003 | pmid = 14633974 | pmc = 289149 | doi = 10.1101/gad.1148603 }} 4. ^{{cite journal | vauthors = Placido A, Sieber F, Gobert A, Gallerani R, Giegé P, Maréchal-Drouard L | title = Plant mitochondria use two pathways for the biogenesis of tRNAHis | journal = Nucleic Acids Research | volume = 38 | issue = 21 | pages = 7711–7 | date = November 2010 | pmid = 20660484 | pmc = 2995067 | doi = 10.1093/nar/gkq646 }} 5. ^{{cite journal | vauthors = Jackman JE, Phizicky EM | title = Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase | journal = Biochemistry | volume = 47 | issue = 16 | pages = 4817–25 | date = April 2008 | pmid = 18366186 | doi = 10.1021/bi702517q }} 6. ^{{cite journal | vauthors = Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S | title = tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 47 | pages = 20305–10 | date = November 2010 | pmid = 21059936 | pmc = 2996709 | doi = 10.1073/pnas.1010436107 }} External links
1 : EC 2.7.7 |
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