EC Number   |
General Information |
Reference  |
|---|
    2.1.2.3 | more |
the enzyme is located at the C-terminus of the bifunctional purine-biosynthesis protein, PurH, whose N-terminus possesses IMP cyclohydrolase activity. Coupling of the two domains is essential for the catalytic process, as the AICAR Tfase reaction favours the reverse direction by itself and the irreversible cyclization of 5-formyl-aminoimidazole-4-carboxamide ribonucleotide to IMP drives formyl transfer in the forward direction |
718506 |
| 2.1.2.3 | metabolism |
aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis |
719415 |
| 2.1.2.3 | metabolism |
aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis. No enzyme complex that generates 10-formyl-5,6,7,8-tetrahydrofolate and immediately channels or furnishes it to AICAR transformylase is needed because the first oxidation product of 10-formyl-5,6,7,8-tetrahydrofolate is 10-formyl-7,8-dihydrofolate that is utilized by this transformylase |
719415 |
| 2.1.2.3 | more |
structure and active site of AICAR transformylase are not consistent with other enzymes that utilize 10-formyl-5,6,7,8-tetrahydrofolate. Methotrexate blockage of the AICAR transformylase process in patients with rheumatoid arthritis suggests that dihydrofolate reductase is involved and is consistent with dihydrofolate and 10-formyl-7,8-dihydrofolate being the product and substrate for AICAR transformylase |
719415 |
| 2.1.2.3 | physiological function |
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase, an enzyme in purine nucleotide biosynthesis de novo, which introduces C2 into the purine ring |
719415 |
| 2.1.2.3 | more |
the enzyme is part of the the bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, ATIC, or PurH |
-, 719985 |
| 2.1.2.3 | malfunction |
inhibition of the enzyme results in depletion of purine nucleotides |
736619 |
| 2.1.2.3 | physiological function |
the enzyme is involved in purine nucleotide biosynthesis |
736619 |
| 2.1.2.3 | malfunction |
insulin stimulation and enzyme ATIC knockdown readily increase the level of AMP-activated protein kinase-Thr172 phosphorylation in insulin receptor complexes. Enzyme ATIC, protein-tyrosine phosphatase-like A domain-containing protein 1, and AMP-activated protein kinase knockdown affects insulin receptor internalization in HEK-293 cells |
736802 |
| 2.1.2.3 | malfunction |
insulin stimulation and enzyme ATIC knockdown readily increase the level of AMPK-Thr172 phosphorylation in insulin receptor complexes |
736802 |
