KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0017 | - |
p-tRNAHis | pH 7.5, 22°C | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
p-tRNAHis + ATP + GTP | Saccharomyces cerevisiae | the G(-1) residue is both necessary and sufficient for aminoacylation of tRNA by histidyl-tRNA synthetase in vitro and is required for aminoacylation in vivo | pppGp-tRNAHis + AMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P53215 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
p-tRNAHis + ATP + GTP | the G(-1) residue is both necessary and sufficient for aminoacylation of tRNA by histidyl-tRNA synthetase in vitro and is required for aminoacylation in vivo | Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? | |
p-tRNAHis + ATP + GTP | Thg1 is more than 10000-fold more selective for its cognate substrate tRNAHis than for the noncognate substrate tRNAPhe. Alteration of this anticodon in tRNAHis completely abrogates Thg1 activity, and the introduction of this GUG anticodon to tRNAPhe or tRNAGly results in significant Thg1 activity | Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
THG1 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0122 | - |
p-tRNAHis | pH 7.5, 22°C | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |