EC Number   |
General Information |
Reference |
|---|
    2.1.2.3 | metabolism |
the enzyme AICAR-transformylase/IMP cyclohydrolase (ATIC) catalyzes the last two steps of purine de novo synthesis. High glucose up-regulates the expression and activity of the enzyme and increases the levels of reactive oxygen species and methylglyoxal-derived advanced glycation end products. Overexpression of the enzyme (atic-1) decreases the lifespan and head motility and increases neuronal damage under both standard and high glucose conditions. Inhibition of atic-1 expression, by RNAi, under high glucose is associated with increased lifespan and head motility and reduced neuronal damage, reactive oxygen species, and methylglyoxal-derived advanced glycation end product accumulation. The enzyme (atic-1) is involved in glucotoxic effects under high glucose conditions, either by blocked atic-1 expression or via induction of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) and AMP-activated kinase (AMPK) induction |
757213 |
| 2.1.2.3 | metabolism |
the enzyme is involved in the folate recycling pathway |
-, 757625 |
| 2.1.2.3 | more |
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide is a is a potent allosteric AMPK activator |
736802 |
| 2.1.2.3 | more |
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide is a is a potent allosteric AMPK activator. Insulin receptor autophosphorylation in isolated endosomes incubated in the presence of purified enzyme ATIC |
736802 |
| 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 | 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 | 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 | 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 | physiological function |
enzyme overexpression decreases the median lifespan from 23.6 to 20.6 days compared with control nematodes under standard conditions |
757213 |
| 2.1.2.3 | physiological function |
the bicuntional enzyme ATIC accelerates wound healing of NIH-3T3 fibroblasts by inducing proliferation and migration |
756701 |
