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Literature summary for 2.7.7.B5 extracted from
- Direct evidence that thil is an ATP pyrophosphatase for the adenylation of uridine in 4-thiouridine biosynthesis (2008), ChemBioChem, 9, 1879-1882.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D189A | mutation eliminates in vivo function of the enzyme | Escherichia coli |
| K321M | mutation eliminates in vivo function of the enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
ATP | pH 7.5, 22°C | Escherichia coli |  |
| 0.84 | - |
GTP | pH 7.5, 22°C | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | ThiI is involved in the modification of uridine to 4-thiouridine | ? | - |
? | |
| additional information | Escherichia coli | ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | ThiI is involved in the modification of uridine to 4-thiouridine | Escherichia coli | ? | - |
? | |
| additional information | ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine | Escherichia coli | ? | - |
? | |
| tRNA-uridine + ATP | - |
Escherichia coli | adenylated-trNA-uridine + diphosphate | - |
? | |
| tRNA-uridine + ATP | based upon sequence alignments, ThiI shares a unique P-loop motif with the PPi synthetase family. ThiI very likely catalyzes the adenylation of a substrate, probably a molecule bearing a carbonyl oxygen | Escherichia coli | adenylated-trNA-uridine + diphosphate | - |
? | |
| tRNA-uridine + GTP | kcat/Km for GTP is about 6fold lower than the value for ATP | Escherichia coli | adenylated-trNA-uridine + diphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ThiI | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.113 | - |
GTP | pH 7.5, 22°C | Escherichia coli | |
| 0.604 | - |
ATP | pH 7.5, 22°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
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Release 2023.1 (January 2023)
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