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Literature summary for 2.7.7.79 extracted from
- tRNAHis guanylyltransferase catalyzes a 3'-5' polymerization reaction that is distinct from G-1 addition (2006), Proc. Natl. Acad. Sci. USA, 103, 8640-8645.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| p-tRNAHis + ATP + GTP | Saccharomyces cerevisiae | - |
pppGp-tRNAHis + AMP + diphosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme also catalyzes 3'-5' extension of a polynucleotude chain by multiple nucleotides. Unlike the addition of G(-1), the reverse polymerisation activity is template-dependent, recognizing G*C WatsonCrick base pairs. Moreover, reverse polymerization is not specific for tRNAHis or for starting at the (-1) position of tRNA, provided that the activated (triphosphorylated) form of the tRNA substrate is used in the assays | Saccharomyces cerevisiae | ? | - |
? | |
| p-tRNAHis + ATP + GTP | - |
Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? | |
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