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Literature summary for 2.7.7.79 extracted from
- Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties (1991), J. Biol. Chem., 266, 22826-22831.
General Stability
| General Stability | Organism |
|---|---|
| the enzyme shows a drastically shortened half-life in the absence of divalent metal ions | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5,5'-dithiobis(2-nitrobenzoic)acid | progressive loss of activity with increasing amounts of DTNB. Thus, sulfhydryl groups are involved in maintaining the active state of the enzyme or are involved in the mechanism | Saccharomyces cerevisiae |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Co2+ is 13% compared to the activity in presence of 10 mM Mg2+ | Saccharomyces cerevisiae | |
| Mg2+ | the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Maximal activity by 10 mM Mg2+ | Saccharomyces cerevisiae | |
| Mn2+ | the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Mn2+ is 70% compared to the activity in presence of 10 mM Mg2+ | Saccharomyces cerevisiae | |
| Zn2+ | the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Zn2+ is 15% compared to the activity in presence of 10 mM Mg2+ | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 58000 | - |
2 * 58000, SDS-PAGE | Saccharomyces cerevisiae |
| 120000 | - |
gel filtration | Saccharomyces cerevisiae |
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 | P53215 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| p-tRNAHis + ATP + GTP | - |
Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? | |
| p-tRNAHis + ATP + GTP | among all acceptor tRNAs in unfractionatedt RNA only tRNAHis is a substrate for the purified enzyme. tRNA from plant and prokaryotes are better substrates than mammalian and insect tRNAs | Saccharomyces cerevisiae | pppGp-tRNAHis + AMP + diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 58000, SDS-PAGE | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| histidine tRNA guanylyltransferase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Saccharomyces cerevisiae |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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