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Literature summary extracted from

  • Verma, P.; Kar, B.; Varshney, R.; Roy, P.; Sharma, A.
    Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis (2017), FEBS J., 284, 4233-4261 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.2.3 drug development the enzyme is an important drug target Staphylococcus lugdunensis
3.5.4.10 drug development the enzyme is an important drug target Staphylococcus lugdunensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.3
-
 Staphylococcus lugdunensis
2.1.2.3 expressed in Escherichia coli BL21(DE3) cells Staphylococcus lugdunensis
3.5.4.10
-
 Staphylococcus lugdunensis

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.3 H256A inactive Staphylococcus lugdunensis
2.1.2.3 H256A complete loss of activity, mutation lowers the thermostability Staphylococcus lugdunensis
2.1.2.3 K255A inactive Staphylococcus lugdunensis
2.1.2.3 K255A complete loss of activity, mutation lowers the thermostability Staphylococcus lugdunensis
2.1.2.3 K255R mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C Staphylococcus lugdunensis
2.1.2.3 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
2.1.2.3 N415A the mutation results in decrease in enzyme activity as compared with wild type enzyme Staphylococcus lugdunensis
3.5.4.10 H256A complete loss of activity, mutation lowers the thermostability Staphylococcus lugdunensis
3.5.4.10 K255A complete loss of activity, mutation lowers the thermostability Staphylococcus lugdunensis
3.5.4.10 K255R mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C Staphylococcus lugdunensis
3.5.4.10 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.3 0.0021
-
 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide at pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis
2.1.2.3 0.03243
-
 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide at pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis
2.1.2.3 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
2.1.2.3 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
2.1.2.3 0.138
-
 10-formyltetrahydrofolate full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis
2.1.2.3 0.13824
-
 10-formyltetrahydrofolate at pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis
2.1.2.3 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
3.5.4.10 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
3.5.4.10 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.3 106000
-
 gel filtration Staphylococcus lugdunensis
3.5.4.10 106000
-
 gel filtration Staphylococcus lugdunensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.3 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
2.1.2.3 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
3.5.4.10 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Staphylococcus lugdunensis
-
 IMP + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.3 Staphylococcus lugdunensis
-
-
-
2.1.2.3 Staphylococcus lugdunensis A0A133Q8U5
-
-
3.5.4.10 Staphylococcus lugdunensis A0A133Q8U5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.3
-
 Staphylococcus lugdunensis
2.1.2.3 CM-Sepharose column chromatography, DEAE-Sepharose column chromatography, octyl Sepharose column chromatography, and Superdex S200 gel filtration Staphylococcus lugdunensis
3.5.4.10
-
 Staphylococcus lugdunensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.3 0.0496
-
 crude enzyme, at pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis
2.1.2.3 0.973
-
 after 19.62fold purification, at pH 7.4, temperature not specified in the publication Staphylococcus lugdunensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.3 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
2.1.2.3 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
2.1.2.3 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
2.1.2.3 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
-
 ?
3.5.4.10 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 Staphylococcus lugdunensis IMP + H2O
-
 ?
3.5.4.10 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

EC Number Subunits Comment Organism
2.1.2.3 ? x * 35000-37000, SDS-PAGE Staphylococcus lugdunensis
2.1.2.3 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
3.5.4.10 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

EC Number Synonyms Comment Organism
2.1.2.3 AICAR TFase
-
 Staphylococcus lugdunensis
2.1.2.3 AICAR transformylase
-
 Staphylococcus lugdunensis
2.1.2.3 AICAR transformylase/IMP cyclohydrolase
-
 Staphylococcus lugdunensis
2.1.2.3 ATIC
-
 Staphylococcus lugdunensis
2.1.2.3 ATIC bifunctional enzyme showing 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities Staphylococcus lugdunensis
3.5.4.10 AICAR transformylase/IMP cyclohydrolase
-
 Staphylococcus lugdunensis
3.5.4.10 ATIC
-
 Staphylococcus lugdunensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.3 35
-
-
 Staphylococcus lugdunensis
2.1.2.3 35
-
 AICAR transformylase activity of the bifunctional enzyme Staphylococcus lugdunensis
3.5.4.10 37
-
 IMP cyclohydrolase activity of the bifunctional enzyme Staphylococcus lugdunensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.3 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
2.1.2.3 25 45 more than 60% activity between 25 and 45°C Staphylococcus lugdunensis
3.5.4.10 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.3 10 40 the enzyme retains stable at 10-40°C with more than 80% activity remaining after 1 h incubation Staphylococcus lugdunensis
2.1.2.3 42.1
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis
2.1.2.3 44.7
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis
2.1.2.3 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
2.1.2.3 46.9
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis
3.5.4.10 42.1
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis
3.5.4.10 44.7
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis
3.5.4.10 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
3.5.4.10 46.9
-
 three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C Staphylococcus lugdunensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.3 7.8
-
-
 Staphylococcus lugdunensis
2.1.2.3 7.8
-
 AICAR transformylase activity of the bifunctional enzyme Staphylococcus lugdunensis
3.5.4.10 8.4
-
 IMP cyclohydrolase activity of the bifunctional enzyme Staphylococcus lugdunensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.3 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
2.1.2.3 7 9 more than 60% activity between pH 7.0 and 9.0 Staphylococcus lugdunensis
3.5.4.10 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

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.2.3 5.5
-
 1 h, enzyme retains 30% of its AICAR transformylase activity Staphylococcus lugdunensis
2.1.2.3 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
2.1.2.3 6
-
 1 h, enzyme retains 60% of its AICAR transformylase activity Staphylococcus lugdunensis
2.1.2.3 6.5 10 1. quite stable over a broad pH range from 6.5 to 10 Staphylococcus lugdunensis
3.5.4.10 5.5
-
 1 h, enzyme retains 20% of its IMP cyclohydrolase activity Staphylococcus lugdunensis
3.5.4.10 6
-
 1 h, enzyme retains 60% of its IMP cyclohydrolase activity Staphylococcus lugdunensis
3.5.4.10 6.5 10 1 h, quite stable over a broad pH range from 6.5 to 10 Staphylococcus lugdunensis

General Information

EC Number General Information Comment Organism
2.1.2.3 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
2.1.2.3 physiological function the bicuntional enzyme ATIC accelerates wound healing of NIH-3T3 fibroblasts by inducing proliferation and migration Staphylococcus lugdunensis
3.5.4.10 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