Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | 20 mM (7fold excess over ATP), 94% inhibition | Saccharomyces cerevisiae | |
AMP | 20 mM (7fold excess over ATP), complete inhibition | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
p-tRNAHis + ATP + GTP | Saccharomyces cerevisiae | the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase | pppG-p-tRNAHis + AMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P53215 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
App-tRNAHis + GTP = pppGp-tRNAHis + AMP | (1b) | Saccharomyces cerevisiae | |
p-tRNAHis + ATP + GTP + H2O = pGp-tRNAHis + AMP + 2 diphosphate | overall reaction | Saccharomyces cerevisiae | |
p-tRNAHis + ATP = App-tRNAHis + diphosphate | (1a) | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
p-tRNAHis + ATP + dGTP | dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme | Saccharomyces cerevisiae | ? | - |
? | |
p-tRNAHis + ATP + GDP | dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme | Saccharomyces cerevisiae | ? | - |
? | |
p-tRNAHis + ATP + GTP | the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase | Saccharomyces cerevisiae | pppG-p-tRNAHis + AMP + diphosphate | - |
? | |
p-tRNAHis + ATP + GTP | during the first step ATP is cleaved to AMP and diphosphate creating adenylylated enzyme. In a second step the activated enzyme forms a stable complex with its cognate tRNA substrate. The 5'-phosphate of the tRNA is adenylylated by nucleotide transfer from the adenylylated guanylyltransferase to form A(5')pp(5') at the 5'-end of the tRNA. Finally, the 3'-hydroxyl of GTP adds to the activated 5' terminus of the tRNA with the release of AMP. dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme | Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? | |
p-tRNAHis + dATP + GTP | 30% of the activity compared to ATP | Saccharomyces cerevisiae | pppGp-tRNAHis + dAMP + diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
histidine tRNA guanylyltransferase | - |
Saccharomyces cerevisiae |
TGT | - |
Saccharomyces cerevisiae |