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malfunction
inhibition of the enzyme results in depletion of purine nucleotides
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
malfunction
Q6IN16
insulin stimulation and enzyme ATIC knockdown readily increase the level of AMPK-Thr172 phosphorylation in insulin receptor complexes
malfunction
the ATIC rs2372536 GG enzyme genotype is associated with improved clinical remission in juvenile idiopathic arthritis during methotrexate therapy, only one of the ATIC single nucleotide polymorphisms show any trend toward methotrexate response in an independent cohort of North American juvenile idiopathic arthritis children
malfunction
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
malfunction
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growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
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metabolism
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aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis
metabolism
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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
metabolism
last and rate-limiting enzyme of the de novo purine synthesis pathway
metabolism
Q6IN16
last and rate-limiting enzyme of the de novo purine synthesis pathway
metabolism
last enzyme of the de novo purine synthesis pathway. The enzyme plays a central role in insulin signaling and the Golgi/endosomes protein network
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
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
metabolism
the enzyme is involved in the folate recycling pathway
metabolism
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the enzyme is involved in the folate recycling pathway
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physiological function
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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
physiological function
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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
physiological function
the enzyme 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase plays a central role in insulin signaling and the Golgi/endosomes protein network, compartmentalization in vivo of involved enzymes in response to insulin, kinetics of the localization, overview
physiological function
Q6IN16
the enzyme 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase plays a central role in insulin signaling and the Golgi/endosomes protein network, compartmentalization in vivo of involved enzymes in response to insulin, kinetics of the localization, overview
physiological function
the enzyme is involved in purine nucleotide biosynthesis
physiological function
enzyme overexpression decreases the median lifespan from 23.6 to 20.6 days compared with control nematodes under standard conditions
physiological function
the bicuntional enzyme ATIC accelerates wound healing of NIH-3T3 fibroblasts by inducing proliferation and migration
additional information
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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
additional information
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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
additional information
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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
additional information
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the enzyme is part of the the bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, ATIC, or PurH
additional information
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide is a is a potent allosteric AMPK activator
additional information
Q6IN16
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
additional information
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the enzyme is part of the the bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase, ATIC, or PurH
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