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Literature summary for 2.1.2.3 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 |
| expressed in Escherichia coli BL21(DE3) cells | Staphylococcus lugdunensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H256A | inactive | Staphylococcus lugdunensis |
| H256A | complete loss of activity, mutation lowers the thermostability | Staphylococcus lugdunensis |
| K255A | inactive | 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 |
| N415A | the mutation results in decrease in enzyme activity as compared with wild type enzyme | Staphylococcus lugdunensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0021 | - |
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | at pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis |  |
| 0.03243 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | at pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
| 0.03468 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
| 0.13437 | - |
10-formyltetrahydrofolate | AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
| 0.138 | - |
10-formyltetrahydrofolate | full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
| 0.13824 | - |
10-formyltetrahydrofolate | at pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis | |
| 0.3243 | - |
5-amino-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. |
|---|---|---|---|---|---|---|
| 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | Staphylococcus lugdunensis | - |
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
r | |
| tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | Staphylococcus lugdunensis | - |
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus lugdunensis | - |
- |
- |
| Staphylococcus lugdunensis | A0A133Q8U5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus lugdunensis |
| CM-Sepharose column chromatography, DEAE-Sepharose column chromatography, octyl Sepharose column chromatography, and Superdex S200 gel filtration | Staphylococcus lugdunensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0496 | - |
crude enzyme, at pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis |
| 0.973 | - |
after 19.62fold purification, at pH 7.4, temperature not specified in the publication | Staphylococcus lugdunensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
Staphylococcus lugdunensis | tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
r | |
| 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | the two activities of the bifunctional AICAR transformylase/IMP cyclohydrolase reside on separate domains | Staphylococcus lugdunensis | tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
r | |
| tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
Staphylococcus lugdunensis | 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
r | |
| tetrahydrofolate + 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 | 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 35000-37000, SDS-PAGE | Staphylococcus lugdunensis |
| 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 TFase | - |
Staphylococcus lugdunensis |
| AICAR transformylase | - |
Staphylococcus lugdunensis |
| AICAR transformylase/IMP cyclohydrolase | - |
Staphylococcus lugdunensis |
| ATIC | - |
Staphylococcus lugdunensis |
| ATIC | bifunctional enzyme showing 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities | Staphylococcus lugdunensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
- |
Staphylococcus lugdunensis |
| 35 | - |
AICAR transformylase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 50 | 20°C: about 40% of maximal activity, 50°C: about 40% of maximal activity, AICAR transformylase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
| 25 | 45 | more than 60% activity between 25 and 45°C | Staphylococcus lugdunensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 40 | the enzyme retains stable at 10-40°C with more than 80% activity remaining after 1 h incubation | Staphylococcus lugdunensis |
| 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 |
|---|---|---|---|
| 7.8 | - |
- |
Staphylococcus lugdunensis |
| 7.8 | - |
AICAR transformylase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9.5 | pH 6.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity, AICAR transformylase activity of the bifunctional enzyme | Staphylococcus lugdunensis |
| 7 | 9 | more than 60% activity between pH 7.0 and 9.0 | Staphylococcus lugdunensis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
1 h, enzyme retains 30% of its AICAR transformylase activity | Staphylococcus lugdunensis |
| 6 | 10 | the enzyme retains stable at pH 7.0-10.0 with more than 80% activity remaining after 1 h incubation. The enzyme retains 60% of its activity at pH 6.0, but there is a sharp decline in the enzyme activity thereafter at lower pH | Staphylococcus lugdunensis |
| 6 | - |
1 h, enzyme retains 60% of its AICAR transformylase activity | Staphylococcus lugdunensis |
| 6.5 | 10 | 1. 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 |
| physiological function | the bicuntional enzyme ATIC accelerates wound healing of NIH-3T3 fibroblasts by inducing proliferation and migration | Staphylococcus lugdunensis |
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