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Literature summary for 3.5.4.10 extracted from
- Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis (2017), FEBS J., 284, 4233-4261 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is an important drug target | Staphylococcus lugdunensis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Staphylococcus lugdunensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H256A | complete loss of activity, mutation lowers the thermostability | Staphylococcus lugdunensis |
| K255A | complete loss of activity, mutation lowers the thermostability | Staphylococcus lugdunensis |
| K255R | mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C | Staphylococcus lugdunensis |
| N415A | decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability | Staphylococcus lugdunensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00184 | - |
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | IMP cyclohydrolase of the domain truncation mutant pET-28c-IMPCH, pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis |  |
| 0.21 | - |
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 106000 | - |
gel filtration | Staphylococcus lugdunensis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | Staphylococcus lugdunensis | - |
IMP + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus lugdunensis | A0A133Q8U5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus lugdunensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
Staphylococcus lugdunensis | IMP + H2O | - |
? | |
| 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | the two activities of the bifunctional AICAR transformylase/IMP cyclohydrolase reside on separate domains | Staphylococcus lugdunensis | IMP + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 54000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking studies, the purified recombinant enzyme and its truncated domains exist mainly in dimeric form | Staphylococcus lugdunensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AICAR transformylase/IMP cyclohydrolase | - |
Staphylococcus lugdunensis |
| ATIC | - |
Staphylococcus lugdunensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
IMP cyclohydrolase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 50 | 20°C: about 45% of maximal activity, 50°C: about 40% of maximal activity, IMP cyclohydrolase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42.1 | - |
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C | Staphylococcus lugdunensis |
| 44.7 | - |
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C | Staphylococcus lugdunensis |
| 45 | - |
10 min, the bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC) is stable at lower temperatures and both the activities start declining after 45°C | Staphylococcus lugdunensis |
| 46.9 | - |
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C | Staphylococcus lugdunensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.4 | - |
IMP cyclohydrolase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | pH 6.0: about 60% of maximal activity, pH 10.0: about 60% of maximal activity, IMP cyclohydrolase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
1 h, enzyme retains 20% of its IMP cyclohydrolase activity | Staphylococcus lugdunensis |
| 6 | - |
1 h, enzyme retains 60% of its IMP cyclohydrolase activity | Staphylococcus lugdunensis |
| 6.5 | 10 | 1 h, quite stable over a broad pH range from 6.5 to 10 | Staphylococcus lugdunensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) catalyzes final two steps of purine nucleotide de novo biosynthetic pathway. The cell proliferation activity of the enzyme is observed where it promotes proliferation and viability of NIH 3T3 and RIN-5F cells, exhibits in vitro wound healing in NIH 3T3 fibroblast cells, and rescues RIN-5F cells from the cytotoxic effects of palmitic acid and high glucose | Staphylococcus lugdunensis |
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