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TRNA(His) guanylyltransferase

FieldValue
NametRNA(His) guanylyltransferase
EC_number2.7.7.79

tRNA(His) guanylyltransferase (, histidine tRNA guanylyltransferase, Thg1p, Thg1) is an enzyme with systematic name p-tRNA(His):GTP guanylyltransferase (ATP-hydrolysing). This enzyme catalyses the following chemical reaction

: p-tRNA(His) + ATP + GTP \rightleftharpoons pppGp-tRNA(His) + AMP + diphosphate (overall reaction) : (1a) p-tRNA(His) + ATP \rightleftharpoons App-tRNA(His) + diphosphate : (1b) App-tRNA(His) + GTP \rightleftharpoons pppGp-tRNA(His) + AMP

The enzyme requires a divalent cation for activity.

Thg1 enzymes are the only nucleic acid polymerases known to be capable of catalyzing nucleotide addition in the 3′–5′ direction.

References

References

  1. (December 1991). "Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism". The Journal of Biological Chemistry.
  2. (December 1991). "Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties". The Journal of Biological Chemistry.
  3. (December 2003). "tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis". Genes & Development.
  4. (November 2010). "Plant mitochondria use two pathways for the biogenesis of tRNAHis". Nucleic Acids Research.
  5. (April 2008). "Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase". Biochemistry.
  6. (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.
  7. (May 2012). "Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily". RNA.
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This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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