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Literature summary for 2.7.7.79 extracted from
- Saccharomyces cerevisiae Thg1 uses 5-pyrophosphate removal to control addition of nucleotides to tRNA(His.) (2014), Biochemistry, 53, 1380-1391.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P53215 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | retention of the 5'-triphosphate is correlated with efficient 3'-5' reverse polymerization. The intrinsic rate of removal of diphosphate from the G-1 residue of base-paired tRNAHis substrates is slow. Rates of diphosphate removal depend on the identity of the NTP included in reactions. The GTP 3'-OH is required to stimulate diphosphate removal | Saccharomyces cerevisiae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| THG1 | - |
Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the diphosphate removal activity under all conditions preferentially acts upon tRNAs containing a U-1:A73 terminating base pair. Although Thg1 can add UTP to create a U:A base pair, it efficiently removes the activated 5'-end from this added nucleotide and effectively terminates subsequent addition reactions. Thg1 exhibits 3'-5' polymerization with some tRNA substrates, but addition of a nucleotide at the -1 position is the preferred reaction | Saccharomyces cerevisiae |
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