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(6R,6S)-10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyl-7,8-dihydropteroylpenta-gamma-glutamate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
7,8-dihydropteroylpenta-gamma-glutarate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
?
10-formyl-7,8-dihydropteroylpenta-gamma-L-glutamate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
dihydrofolic acid pentaglutamate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
?
10-formyl-8-deazafolate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide
8-deazafolate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
?
10-formyl-tetrahydrofolic acid + 5'-phosphoribosyl-5-amino-imidazole-carboxamide
5,6,7,8-tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
-
?
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyldihydrofolic acid pentaglutamate + 5-aminoimidazole-4-carboxamide
?
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-imidazole-4-thiocarboxamide ribonucleotide
tetrahydrofolate + 6-mercaptopurine ribonucleotide
-
-
-
?
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide
-
-
-
-
?
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroylheptaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroylhexaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroylmonoglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylmonoglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroylpentaglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroyltetraglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N10-formyltetrahydropteroyltriglutamate + 5'-phosphoribosyl-5-formamino-4-imidazole carboxamide ribonucleotide
tetrahydorpteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
?
N5,N10-anhydroformyltetrahydrofolic acid + glycinamide ribonucleotide
N10-formyltetrahydrofolic acid + formylglycinamide ribonucleotide
-
-
-
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
-
-
-
r
additional information
?
-
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
-
-
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylas
-
-
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
-
-
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylas
-
-
r
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
precursors for inosinic acid biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
reduced folate cofactor requiring step of de novo purine biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
reduced folate cofactor requiring step of de novo purine biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
Trifolium sp.
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Q6IN16
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
-
-
-
r
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
Trifolium sp.
-
-
-
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
r
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
no activity with N5,N10-methenyl analogues
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
polymorphisms in 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene is not associated with recurrent venous thrombosis risk
-
-
?
additional information
?
-
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
-
-
?
additional information
?
-
the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
-
-
?
additional information
?
-
Q6IN16
the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
additional information
?
-
Trifolium sp.
-
in all organisms studied to date AICARFT activity is accompanied by inosine monophosphate cyclohydrolase located on the same polypeptide encoded by the purH gene
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
N10-formyltetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide ribonucleotide
tetrahydropteroylglutamate + 5'-phosphoribosyl-5-formamido-4-imidazole carboxamide
-
-
-
-
?
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
r
additional information
?
-
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
-
-
r
10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
-
penultimate step of the purine de novo synthesis pathway
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
precursors for inosinic acid biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
reduced folate cofactor requiring step of de novo purine biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
penultimate and final steps in the de novo purine biosynthesis pathway
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
reduced folate cofactor requiring step of de novo purine biosynthesis
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
de novo synthesis of purine nucleotides
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
Trifolium sp.
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Q6IN16
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
additional information
?
-
-
polymorphisms in 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene is not associated with recurrent venous thrombosis risk
-
-
?
additional information
?
-
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
-
-
?
additional information
?
-
the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
-
-
?
additional information
?
-
-
10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase. Bioactivity of the unnatural isomer [6R]-5-formyltetrahydrofolate is in vivo converted to 10-formyl-7,8-dihydrofolate and serves thus as a substrate
-
-
?
additional information
?
-
Q6IN16
the enzyme forms a complex with its substrate via the phosphate-binding pocket of the IMP cyclohydrolase (IMPCH) domain (residues 1-599)
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(2RS)-N-[4-{1-(acetamideoxy)-3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{1-(acetoxy)-3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1,1-(dimethoxy)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(1,1-bromoacetoxy)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(1,1-dimethoxyacetoxy)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(ethoxalyoxy) prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(formyloxy)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(hydroxy)prop-2-yl}benzoyl]-L-glutamic acid
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(2RS)-N-[4-{3-(2-amino-3,4-dihydro-4-oxo-quinazolin-6-yl)-1-(pyruvoyloxy)prop-2-yl}benzoyl]-L-glutamic acid
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(6S/R)-5,10-dideaza-5,6,7,8,-tetrahydrofolate
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(S)-2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)pentanedioic acid
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(S)-2-(4-(2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl)benzamido)pentanedioic acid
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(S)-2-(4-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)propyl)benzamido)pentanedioic acid
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(S)-2-(4-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)butyl)benzamido)pentanedioic acid
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(S)-2-(4-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)pentyl)benzamido)pentanedioic acid
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(S)-2-(4-(6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)hexyl)benzamido)pentanedioic acid
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(S)-2-(5-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)propyl)thiophene-2-carboxamido)pentanedioic acid
inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
(S)-2-(5-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)butyl)thiophene-2-carboxamido)pentanedioic acid
inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
(S)-2-[2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-acetylamino]-pentanedioic acid
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(S)-2-[2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-acetylamino]-pentanedioic acid
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(S)-2-[3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-propionylamino]-pentanedioic acid
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(S)-2-[3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-propionylamino]-pentanedioic acid
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(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-benzoylamino]-pentanedioic acid
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(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-butyrylamino]-pentanedioic acid
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(S)-2-[5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoylamino]-pentanedioic acid
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(S)-2-[6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoylamino]-pentanedioic acid
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1-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetyl]-piperidine-4-carboxylic acid (pyridin-3-ylmethyl)-amide
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10-formyl-5,6,7,8-tetrahydropteroylpenta-gamma-glutamate
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10-formyl-5,8,10-trideazafolate
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10-formylfolic acid pentaglutamate
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competitive inhibitor
2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-N-[[(pyridin-3-ylmethyl)-carbamoyl]-methyl]-acetamide
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2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-2-ylmethyl-acetamide
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2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-3-ylmethyl-acetamide
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2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-4-ylmethyl-acetamide
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2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
Acid Yellow 54, 326203-A, competitive against 10-formyltetrahydrofolate, IC50: 0.012 mM, inhibitor partially blocks the cofactor binding site
2-[[([4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorophenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]phenyl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
2-[[([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,5-dihydrothiophen-2-yl]carbonyl)amino]methyl]-3-methylidenebutanedioic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
3-[(4-cyanobenzene-1-sulfonyl)amino]benzamide
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3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-propionamide
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3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-2-ylmethyl-propionamide
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3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-3-ylmethyl-propionamide
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3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-ethylsulfanyl]-N-pyridin-4-ylmethyl-propionamide
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4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide
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inhibition of thymidylate synthase, as well as glycinamide ribonucleotide formyltransferase and ribonucleotide formyltransferase. Growth inhibition of 4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide toward KB cells results in cytotoxicity and G1/G2-phase accumulation, and is partially protected by excess thymidine and adenosine, but is completely reversed in the combination of thymidine and adenosine
4-8[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)acetamido]methyl]-N-[(pyridin-3-yl)methyl]benzamide
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4-amino-10-methylpteroyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
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methotrexate polyglutamate, competitive inhibitor
4-amino-10-methylpteroylglutamic acid
4-amino-4-deoxy-5,8,10-trideazapteroyl-D,L-40-methyleneglutamic acid
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weak inhibition of enzymes of folate metabolism relevant to rheumatoid arthritis therapy such as thymidylate synthase EC 2.1.1.45, two formyltransferases of purine biosynthesis EC 2.1.2.2 and EC 2.1.2.3, and 5,10-methylenetetrahydrofolate reductase EC 1.5.1.20. Potent inhibition of dihydrofolate reductase
4-chloro-N-(1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)benzene-1-sulfonamide
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4-cyano-N-(1-oxo-1,2-dihydroisoquinolin-7-yl)benzene-1-sulfonamide
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4-cyano-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)benzene-1-sulfonamide
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4-cyano-N-phenylbenzene-1-sulfonamide
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4-N-allyl-5-aminoimidazole-4-carboxamide ribonucleotide
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4-N-methyl-5-aminoimidazole-4-carboxamide ribonucleotide
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4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-cyclohexanecarboxylic acid (pyridin-3-ylmethyl)-amide
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4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-benzamide
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4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-butyramide
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5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
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product inhibitor
5-(5,5-dimethyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
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5-(5-ethyl-5-methyl-6-oxo-1,4-dihydropyridin-3-yl)-N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)thiophene-2-sulfonamide
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5-amino-1-beta-D-ribofuranosylimidazole 5'-phosphate
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5-amino-1-beta-D-ribofuranosylimidazole-4-carbonitrile 5'-phosphate
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5-amino-1-beta-D-ribofuranosylimidazole-4-carboxamidoxime 5'-phosphate
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5-amino-1-beta-D-ribofuranosylimidazole-4-carboxylate 5'-phosphate
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5-amino-4-nitro-1-beta-D-ribofuranosylimidazole 5'-phosphate
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5-amino-4-nitroimidazole ribonucleotide
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5-formyl-5-aminoimidazole-4-carboxamide ribonucleotide
5-[(3R,4S)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
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5-[(3S,4R)-3-fluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
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5-[(4R)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
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5-[(4S)-3,3-difluoro-4-hydroxypyrrolidin-1-yl]-N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)thiophene-2-sulfonamide
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5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoic acid (pyridin-3-ylmethyl)-amide
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6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoic acid (pyridin-3-ylmethyl)-amide
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7,8-dihydropteroylpenta-gamma-glutamate
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Acid Yellow 17
IC50: 0.012 mM
BW1540
sulfamido-bridged 5,8-dideazafolate analogue
BW2315
sulfamido-bridged 5,8-dideazafolate analogue
Cappsin 1
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non-competitive, inhibition of activity by preventing the formation of dimers
Cappsin 2
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some derivatives of Cappepsin are also inhibitory, inhibition of activity by preventing the formation of dimers
dihydrofolic acid pentaglutamate
folic acid pentaglutamate
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competitive inhibitor
N-(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)-4-cyanobenzene-1-sulfonamide
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N-(3-[[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]sulfanyl]propanoyl)-L-glutamic acid
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N-(4-[3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-propyl]benzoyl)-L-glutamic acid
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dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-butyl]benzoyl)-L-glutamic acid
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dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[5-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-pentyl]benzoyl)-L-glutamic acid
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dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[6-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-hexyl]benzoyl)-L-glutamic acid
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dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
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N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamylglutamic acid
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N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
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N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-(4-hydroxypiperidin-1-yl)thiophene-2-sulfonamide
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N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide
LSN 3213128, potent and selective inhibitor
N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-(6-oxo-1H-pyridin-3-yl)thiophene-2-sulfonamide
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N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3R)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
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N-(6-fluoro-1-oxo-2H-isoquinolin-7-yl)-5-[(3S)-3-hydroxy-1-piperidyl]thiophene-2-sulfonamide
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N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
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N-([[2-(2-amino-4-oxo-4,4a,7,7a-tetrahydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]sulfanyl]acetyl)-L-glutamic acid
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N-[(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)amino]sulfonyl]-phenyl)carbonyl]-L-glutamic acid
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N-[(S)-(4-([(2-amino-4-hydroxy-quinazolin-6-yl)dihydroxy-lambda-4-sulfanyl]amino)phenyl)-hydroxymethyl]-L-glutamic acid
binding structure, docking study and crystal structure analysis
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
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N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
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N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
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N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
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N-[4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
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N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid
inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
inhibits de novo purine nucleotide rather than thymidylate biosynthesis via inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
N10-formyltetrahydropteroylglutamate
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NCI324571-C
IC50: 0.042 mM
NCI324572-F
IC50: 0.012 mM
NCI3262203-A
IC50: 0.012 mM
NCI47729-M
IC50: 0.003 mM
pteroylpenta-gamma-glutamate
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4-amino-10-methylpteroylglutamic acid
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methotrexate, non-competitive inhibitor
4-amino-10-methylpteroylglutamic acid
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methotrexate, non-competitive inhibitor
4-amino-10-methylpteroylglutamic acid
methotrexate, non-competitive inhibitor
4-amino-10-methylpteroylglutamic acid
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methotrexate, non-competitive inhibitor
5-formyl-5-aminoimidazole-4-carboxamide ribonucleotide
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5-formyl-5-aminoimidazole-4-carboxamide ribonucleotide
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Azathioprine
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competitive inhibitor
dihydrofolic acid pentaglutamate
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dihydrofolic acid pentaglutamate
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Ibuprofen
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anti-inflammatory drug
Ibuprofen
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anti-inflammatory drug
methotrexate
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methotrexate
enzyme phosphorylation dampens the methotrexate-mediated transformylase activity inhibition
naproxen
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anti-inflammatory drug
naproxen
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anti-inflammatory drug
pemetrexed
the enzyme is a pharmacologically important target of anticancer drug pemetrexed, an antifolate inhibitor
thioinosinic acid
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competitive inhibitor
additional information
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specific antifolate reagents and nonfolate inhibitors are analogues of cofactor N10-formyltetrahydrofolate and can completely inhibit AICAR Tfase activity
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additional information
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methotrexate, MTX, cannot directly inhibit AICAR transformylase, but blocks the AICAR transformylase process in patients with rheumatoid arthritis
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additional information
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synthesis and antitumor activity of a series of 6-substituted pyrrolo[2,3-d]pyrimidines as potential nonclassical antifolates targeting both thymidylate and purine nucleotide biosynthesis, docking study and molecular modeling using the enzyme's crystal structure in complex with compound BW2315, PDB ID 1PL0. Growth inhibition of human cancer cells by the inhibitors, IC50 values, overview
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additional information
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synthesis of 5-substituted pyrrolo[2,3-d]pyrimidine antifolate inhibitors that acts as a dual inhibitor of GARFTase, EC 2.1.2.2, and AICARFTase principal mechanism of action, overview. 8, with a 4-carbon bridge, is the most active analog and potently inhibits proliferation of folate receptor alpha-expressing Chinese hamster ovary and KB human tumor cells. Molecular modeling and docking studies, overview
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additional information
design and synthesis of a series of 5-substituted thiopheneyl pyrrolo[2,3-d]pyrimidines with varying chain lengths (n = 1-6). The compounds show dual inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, analysis of the unique structure-activity relationship for transport and dual target inhibition, molecular modeling and computational studies using crystal structure of human AICARFTase at 2.55 A resolution, PDB ID 1P4R, overview. No inhibition by N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-([5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophen-2-yl]carbonyl)-L-glutamic acid, N-([5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophen-2-yl]carbonyl)-L-glutamic acid, and (S)-2-(5-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)pentyl)thiophene-2-carboxamido)pentanedioic acid
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additional information
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design and synthesis of a series of 5-substituted thiopheneyl pyrrolo[2,3-d]pyrimidines with varying chain lengths (n = 1-6). The compounds show dual inhibition of both glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, analysis of the unique structure-activity relationship for transport and dual target inhibition, molecular modeling and computational studies using crystal structure of human AICARFTase at 2.55 A resolution, PDB ID 1P4R, overview. No inhibition by N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid, N-([5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophen-2-yl]carbonyl)-L-glutamic acid, N-([5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophen-2-yl]carbonyl)-L-glutamic acid, and (S)-2-(5-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)pentyl)thiophene-2-carboxamido)pentanedioic acid
-
additional information
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an adventitiously active site-bound nucleotide, found in the crystal structures, is identified by NMR and mass spectral analysis as a novel 5-formyl derivative of an earlier intermediate in the biosynthetic pathway 4-carboxy-5-aminoimidazole ribonucleotide. The nucleotide is a cyclohydrolase inhibitor. Binding structure analysis, structure modeling, overview
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Adenocarcinoma
Cellular Pharmacodynamics of a Novel Pyrrolo[3,2-d]pyrimidine Inhibitor Targeting Mitochondrial and Cytosolic One-Carbon Metabolism.
Arthritis
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis.
Arthritis
Association of the 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene with response to methotrexate in juvenile idiopathic arthritis.
Arthritis, Juvenile
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis.
Arthritis, Juvenile
Association of the 5-aminoimidazole-4-carboxamide ribonucleotide transformylase gene with response to methotrexate in juvenile idiopathic arthritis.
Arthritis, Rheumatoid
Association of the ATIC 347 C/G polymorphism with responsiveness to and toxicity of methotrexate in rheumatoid arthritis: a meta-analysis.
Arthritis, Rheumatoid
Effects of methotrexate on nucleotide pools in normal human T cells and the CEM T cell line.
Arthritis, Rheumatoid
Evidence for the hypothesis that 10-formyldihydrofolate is the in vivo substrate for aminoimidazolecarboxamide ribotide transformylase.
Arthritis, Rheumatoid
Metabolism-blocked antifolates as potential anti-rheumatoid arthritis agents: 4-amino-4-deoxy-5,8,10-trideazapteroyl-d,l-4'-methyleneglutamic acid (CH-1504) and its analogs.
Ataxia Telangiectasia
DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.
Breast Neoplasms
Proteomic analysis of human macrophages exposed to hypochlorite-oxidized low-density lipoprotein.
Breast Neoplasms
Targeting tumour proliferation with a small-molecule inhibitor of AICAR transformylase homodimerization.
Carcinogenesis
The Adenosine Monophosphate (AMP) Analog, 5-Aminoimidazole-4-Carboxamide Ribonucleotide (AICAR) Inhibits Hepatosteatosis and Liver Tumorigenesis in a High-Fat Diet Murine Model Treated with Diethylnitrosamine (DEN).
Carcinoma
Identification of a Small Molecule Inhibitor of RAD52 by Structure-Based Selection.
Carcinoma, Hepatocellular
The Adenosine Monophosphate (AMP) Analog, 5-Aminoimidazole-4-Carboxamide Ribonucleotide (AICAR) Inhibits Hepatosteatosis and Liver Tumorigenesis in a High-Fat Diet Murine Model Treated with Diethylnitrosamine (DEN).
Diabetes, Gestational
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Fetal Growth Retardation
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Graft vs Host Disease
Cyclosporine and methotrexate-related pharmacogenomic predictors of acute graft-versus-host disease.
Huntington Disease
AMPK activation protects from neuronal dysfunction and vulnerability across nematode, cellular and mouse models of Huntington's disease.
Huntington Disease
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3.
Infections
The Mesorhizobium loti purB gene is involved in infection thread formation and nodule development in Lotus japonicus.
Insulin Resistance
Serum Is Not Necessary for Prior Pharmacological Activation of AMPK to Increase Insulin Sensitivity of Mouse Skeletal Muscle.
Kidney Failure, Chronic
Podocytes maintain high basal levels of autophagy independent of mtor signaling.
Leukemia
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence, and inhibitors.
Leukemia
Dual effects of pyrazofurin and 3-deazauridine upon pyrimidine and purine biosynthesis in mouse L1210 leukemia.
Lung Injury
AICAR decreases acute lung injury by phosphorylating AMPK and upregulating heme oxygenase-1.
Neoplasms
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3.
Neoplasms
Characterization of a novel AICARFT inhibitor which potently elevates ZMP and has anti-tumor activity in murine models.
Neoplasms
Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening.
Neoplasms
Differential effects of AMPK agonists on cell growth and metabolism.
Neoplasms
Discovery of 6-substituted thieno[2,3-d]pyrimidine analogs as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis in folate receptor expressing human tumors.
Neoplasms
Discovery of N-(6-Fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a Potent and Selective Nonclassical Antifolate Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT) Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model.
Neoplasms
DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.
Neoplasms
Peptide YY (PYY) Is Expressed in Human Skeletal Muscle Tissue and Expanding Human Muscle Progenitor Cells.
Neoplasms
STYK1 promotes autophagy through enhancing the assembly of autophagy-specific class III phosphatidylinositol 3-kinase complex I.
Neoplasms
Targeting tumour proliferation with a small-molecule inhibitor of AICAR transformylase homodimerization.
Nephrosis
Podocytes maintain high basal levels of autophagy independent of mtor signaling.
Ovarian Neoplasms
Activation of AMP-activated Protein Kinase by Metformin Induces Protein Acetylation in Prostate and Ovarian Cancer Cells.
Pre-Eclampsia
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Novel pyrrolo[2,3-d]pyrimidine antifolate TNP-351: cytotoxic effect on methotrexate-resistant CCRF-CEM cells and inhibition of transformylases of de novo purine biosynthesis.
Pregnancy Complications
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Premature Birth
AMP-Activated Protein (AMPK) in Pathophysiology of Pregnancy Complications.
Psoriasis
Outcomes of methotrexate therapy for psoriasis and relationship to genetic polymorphisms.
Sepsis
Activation of AMP-activated protein kinase during sepsis/inflammation improves survival by preserving cellular metabolic fitness.
Starvation
Metabolomics profiling of metformin-mediated metabolic reprogramming bypassing AMPK?.
Tuberculosis
Structural analyses of a purine biosynthetic enzyme from Mycobacterium tuberculosis reveal a novel bound nucleotide.
Tuberous Sclerosis
Podocytes maintain high basal levels of autophagy independent of mtor signaling.
Venous Thrombosis
Associations of common polymorphisms in the thymidylate synthase, reduced folate carrier and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase genes with folate and homocysteine levels and venous thrombosis risk.
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Szabados, E.; Hindmarsh, E.J.; Phillips, L.; Duggleby, R.G.; Christopherson, R.I.
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence and inhibitors
Biochemistry
33
14237-14245
1994
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens
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Rayl, E.A.; Moroson, B.A.; Beardsley, G.P.
The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping
J. Biol. Chem.
271
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1996
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens (P31939), Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
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Hartman, S.C.; Buchanan, J.M.
Biosynthesis of the purines. XXVI. The Identification of the formyl donors of the transformylation reactions
J. Biol. Chem.
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1959
Gallus sp.
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Patrick, T.W.; Crosbie, G.W.
Specificity of 4-aminoimidazole-5-carboxamide ribotide transformylase of Escherichia coli
Biochem. J.
124
31-32
1971
Escherichia coli
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Iwai, K.; Fujisawa, Y.; Suzuki, N.
The accumulation of 5'-phosphoribosyl-5amino-4-imidazolecarboxamide in folate-deficient pea seedlings and the enzymatic reaction in which the compound is involved
Agric. Biol. Chem.
36
398-408
1972
Allium cepa, Columba sp., Daucus carota, Escherichia coli, Gallus sp., Petroselinum crispum, Pisum sativum, Spinacia oleracea, Trifolium sp.
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brenda
Baggott, J.E.; Krumdieck, C.L.
Folylpoly-gamma-glutamates as cosubstrates of 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide formyltransferase
Biochemistry
18
1037-1041
1979
Gallus sp.
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Mueller, W.T.; Benkovic, S.J.
On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver
Biochemistry
20
337-344
1981
Gallus sp., Mus musculus
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Smith, G.K.; Mueller, T.; Benkovic, P.A.; Benkovic, S.J.
On the cofactor specificity of glycinamide ribonucleotide and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase from chicken liver
Biochemistry
20
1241-1245
1981
Gallus sp.
brenda
Baggott, J.E.; Vaughn, W.H.; Hudson, B.B.
Inhibition of 5-aminoimidazole-4-carboxamide ribotide transformylase, adenosine deaminase and 5'-adenylate deaminase by polyglutamates of methotrexate and oxidized folates and by 5-aminoimidazole-4-carboxamide riboside and ribotide
Biochem. J.
236
193-200
1986
Gallus sp., Mus musculus
brenda
Ha, T.; Morgan, S.L.; Vaughn, W.H; Eto, I.; Baggott, J.E.
Detection of inhibition of 5-aminoimidazole-4-carboxamide ribotide transformylase by thioinosinic acid and azathioprine by a new colorimetric assay
Biochem. J.
272
339-342
1990
Gallus sp., Homo sapiens, Mus musculus
brenda
Boger, D.L.; Haynes, N.E.; Warren, M.S.; Gooljarsingh, L.T.; Ramcharan, J.; Kitos, P.A.; Benkovic, S.J.
Functionalized analogues of 5,8,10-trideazafolate as potential inhibitors of GAR Tfase or AICAR Tfase
Bioorg. Med. Chem.
5
1831-1838
1997
Gallus sp.
brenda
Sugita, T.; Aya, H.; Ueno, M.; Ishizuka, T.; Kawashima, K.
Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase
J. Biochem.
122
309-313
1997
Bacillus subtilis, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Reyes, V.M.; Greasley, S.E.; Stura, E.A.; Beardsley, G.P.; Wilson, I.A.
Crystallization and preliminary crystallographic investigations of avian 5-aminoimidazole-4-carboxamide ribonucleotide transformylase-inosine monophosphate cyclohydrolase expressed in Escherichia coli
Acta Crystallogr. Sect. D
56
1051-1054
2000
Gallus sp.
-
brenda
Wall, M.; Shim, J.H.; Benkovic, S.J.
Human AICAR transformylase: Role of the 4-Carboxamide of AICAR in binding and catalysis
Biochemistry
39
11303-11311
2000
Escherichia coli, Homo sapiens
brenda
Shim, J.H.; Wall, M.; Benkovic, S.J.; Diaz, N.; Suarez, D.; Merz, K.M., Jr.
Evaluation of the catalytic mechanism of AICAR transformylase by pH-dependent kinetics, mutagenesis, and quantum chemical calculations
J. Am. Chem. Soc.
123
4687-4696
2001
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Vergis, J.M.; Bulock, K.G.; Fleming, K.G.; Beardsley, G.P.
Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity
J. Biol. Chem.
276
7727-7733
2001
Saccharomyces cerevisiae, Gallus sp., Homo sapiens
brenda
Bulock, K.G.; Beardsley, G.P.; Anderson, K.S.
The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase): A surprising lack of substrate channeling
J. Biol. Chem.
277
22168-22174
2002
Gallus sp., Homo sapiens
brenda
Wolan, D.W.; Greasley, S.E.; Beardsley, G.P.; Wilson, I.A.
Structural insights into the avian AICAR transformylase mechanism
Biochemistry
41
15505-15513
2002
Gallus sp., Homo sapiens
brenda
Cheong, C.G.; Wolan, D.W.; Greasley, S.E.; Horton, P.A.; Beardsley, G.P.; Wilson, I.A.
Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates
J. Biol. Chem.
279
18034-18045
2004
Homo sapiens (P31939), Homo sapiens
brenda
Wolan, D.W.; Greasley, S.E.; Wall, M.J.; Benkovic, S.J.; Wilson, I.A.
Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site
Biochemistry
42
10904-10914
2003
Gallus gallus (P31335)
brenda
Vergis, J.M.; Beardsley, G.P.
Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase
Biochemistry
43
1184-1192
2004
aves, Homo sapiens
brenda
Capps, K.J.; Humiston, J.; Dominique, R.; Hwang, I.; Boger, D.L.
Discovery of AICAR Tfase inhibitors that disrupt requisite enzyme dimerization
Bioorg. Med. Chem. Lett.
15
2840-2844
2005
Homo sapiens
brenda
Xu, L.; Li, C.; Olson, A.J.; Wilson, I.A.
Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening
J. Biol. Chem.
279
50555-50565
2004
Gallus gallus (P31335), Homo sapiens (P31939)
brenda
Li, C.; Xu, L.; Wolan, D.W.; Wilson, I.A.; Olson, A.J.
Virtual screening of human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase against the NCI diversity set by use of AutoDock to identify novel nonfolate inhibitors
J. Med. Chem.
47
6681-6690
2004
Homo sapiens (P31939), Homo sapiens
brenda
Gellekink, H.; Blom, H.J.; den Heijer, M.
Associations of common polymorphisms in the thymidylate synthase, reduced folate carrier and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase genes with folate and homocysteine levels and venous thrombosis
Clin. Chem. Lab. Med.
45
471-476
2007
Homo sapiens
brenda
Axelrod, H.L.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Elsliger, M.; Abdubek, P.; Ambing, E.; Astakhova, T.; Carlton, D.; Chiu, H.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Quijano, K.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon. A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 ANG. resolution
Proteins Struct. Funct. Bioinform.
71
1042-1049
2008
Thermotoga maritima
brenda
Boccalatte, F.E.; Voena, C.; Riganti, C.; Bosia, A.; DAmico, L.; Riera, L.; Cheng, M.; Ruggeri, B.; Jensen, O.N.; Goss, V.L.; Lee, K.; Nardone, J.; Rush, J.; Polakiewicz, R.D.; Comb, M.J.; Chiarle, R.; Inghirami, G.
The enzymatic activity of 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase is enhanced by NPM-ALK: new insights in ALK-mediated pathogenesis and the treatment of ALCL
Blood
113
2776-2790
2009
Homo sapiens (P31939)
brenda
McGuire, J.J.; Haile, W.H.
Metabolism-blocked antifolates as potential anti-rheumatoid arthritis agents: 4-amino-4-deoxy-5,8,10-trideazapteroyl-D,L-4-methyleneglutamic acid (CH-1504) and its analogs
Biochem. Pharmacol.
77
1161-1172
2009
Homo sapiens
brenda
Deng, Y.; Zhou, X.; Kugel Desmoulin, S.; Wu, J.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Synthesis and biological activity of a novel series of 6-substituted thieno[2,3-d]pyrimidine antifolate inhibitors of purine biosynthesis with selectivity for high affinity folate receptors over the reduced folate carrier and proton-coupled folate transpo
J. Med. Chem.
52
2940-2951
2009
Homo sapiens
brenda
Qiu, X.; Yuan, Y.; Gao, Y.
Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli
Acta Crystallogr. Sect. F
67
1590-1594
2011
Escherichia coli
brenda
Baggott, J.E.; Tamura, T.
Evidence for the hypothesis that 10-formyldihydrofolate is the in vivo substrate for aminoimidazolecarboxamide ribotide transformylase
Exp. Biol. Med. (Maywood)
235
271-277
2010
Homo sapiens, Rattus norvegicus
brenda
Le Nours, J.; Bulloch, E.M.; Zhang, Z.; Greenwood, D.R.; Middleditch, M.J.; Dickson, J.M.; Baker, E.N.
Structural analyses of a purine biosynthetic enzyme from Mycobacterium tuberculosis reveal a novel bound nucleotide
J. Biol. Chem.
286
40706-40716
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Liu, Y.; Zhang, C.; Zhang, H.; Li, M.; Yuan, J.; Zhang, Y.; Zhou, J.; Guo, H.; Zhao, L.; Du, Y.; Wang, L.; Ren, L.
Synthesis and antitumor activity of a novel series of 6-substituted pyrrolo[2,3-d]pyrimidines as potential nonclassical antifolates targeting both thymidylate and purine nucleotide biosynthesis
Eur. J. Med. Chem.
93
142-155
2015
Homo sapiens
brenda
Mitchell-Ryan, S.; Wang, Y.; Raghavan, S.; Ravindra, M.P.; Hales, E.; Orr, S.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Discovery of 5-substituted pyrrolo[2,3-d]pyrimidine antifolates as dual-acting inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis: Implications of inhibiting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase to AMPK activation and anti-tumor activity
J. Med. Chem.
56
10016-10032
2013
Homo sapiens
brenda
Wang, Y.; Mitchell-Ryan, S.; Raghavan, S.; George, C.; Orr, S.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Novel 5-substituted pyrrolo[2,3-d]pyrimidines as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase and as potential antitumor agents
J. Med. Chem.
58
1479-1493
2015
Homo sapiens (P31939), Homo sapiens
brenda
Boutchueng-Djidjou, M.; Collard-Simard, G.; Fortier, S.; Hebert, S.S.; Kelly, I.; Landry, C.R.; Faure, R.L.
The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC) plays a central role in insulin signaling and the Golgi/endosomes protein network
Mol. Cell. Proteomics
14
1079-1092
2015
Homo sapiens (P31939), Rattus norvegicus (Q6IN16)
brenda
Pastore, S.; Stocco, G.; Moressa, V.; Zandona, L.; Favretto, D.; Malusa, N.; Decorti, G.; Lepore, L.; Ventura, A.
5-Aminoimidazole-4-carboxamide ribonucleotide-transformylase and inosine-triphosphate-pyrophosphatase genes variants predict remission rate during methotrexate therapy in patients with juvenile idiopathic arthritis
Rheumatol. Int.
35
619-627
2015
Homo sapiens (P31939), Homo sapiens
brenda
Witkowska, D.; Cox, H.L.; Hall, T.C.; Wildsmith, G.C.; Machin, D.C.; Webb, M.E.
Analysis of substrate binding in individual active sites of bifunctional human ATIC
Biochim. Biophys. Acta
1866
254-263
2018
Homo sapiens
brenda
Davis, B.W.; Aumiller, W.M.; Hashemian, N.; An, S.; Armaou, A.; Keating, C.D.
Colocalization and sequential enzyme activity in aqueous biphasic systems experiments and modeling
Biophys. J.
109
2182-2194
2015
Homo sapiens
brenda
Liu, Y.; Li, M.; Zhang, H.; Yuan, J.; Zhang, C.; Zhang, K.; Guo, H.; Zhao, L.; Du, Y.; Wang, L.; Ren, L.
Design, synthesis and biological evaluation of 6-substituted pyrrolo[2,3-d]pyrimidines as dual inhibitors of TS and AICARFTase and as potential antitumor agents
Eur. J. Med. Chem.
115
245-256
2016
Homo sapiens
brenda
Xing, R.; Zhang, H.; Yuan, J.; Zhang, K.; Li, L.; Guo, H.; Zhao, L.; Zhang, C.; Li, S.; Gao, T.; Liu, Y.; Wang, L.
Novel 6-substituted benzoyl and non-benzoyl straight chain pyrrolo[2,3-d]pyrimidines as potential antitumor agents with multitargeted inhibition of TS, GARFTase and AICARFTase
Eur. J. Med. Chem.
139
531-541
2017
Homo sapiens
brenda
Verma, P.; Kar, B.; Varshney, R.; Roy, P.; Sharma, A.
Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis
FEBS J.
284
4233-4261
2017
Staphylococcus lugdunensis, Staphylococcus lugdunensis (A0A133Q8U5)
brenda
Markandeyan, D.; Kannaiyan, S.; Suresh, S.; Nimmakayala, R.; Ilamurugan, R.; Santhalingam, K.; Paul, B.
Virtual screening of phytochemicals for methotrexate like dihydrofolate reductase and aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase inhibitory property using Molegro virtual docker
Int. J. Pharm. Pharm. Sci.
8
83-87
2016
Homo sapiens (P31939)
-
brenda
Riedinger, C.; Mendler, M.; Schlotterer, A.; Fleming, T.; Okun, J.; Hammes, H.P.; Herzig, S.; Nawroth, P.P.
High-glucose toxicity is mediated by AICAR-transformylase/IMP cyclohydrolase and mitigated by AMP-activated protein kinase in Caenorhabditis elegans
J. Biol. Chem.
293
4845-4859
2018
Caenorhabditis elegans, Caenorhabditis elegans (Q95QQ4)
brenda
Fales, K.R.; Njoroge, F.G.; Brooks, H.B.; Thibodeaux, S.; Torrado, A.; Si, C.; Toth, J.L.; Mc Cowan, J.R.; Roth, K.D.; Thrasher, K.J.; Frimpong, K.; Lee, M.R.; Dally, R.D.; Shepherd, T.A.; Durham, T.B.; Margolis, B.J.; Wu, Z.; Wang, Y.; Atwell, S.; Wang, J.; Hui, Y.H.; Meier, T.I.; Konicek, S.A.; Geeganage, S.
Discovery of N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a potent and selective nonclassical antifolate aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT) inhibitor
J. Med. Chem.
60
9599-9616
2017
Homo sapiens (P31939)
brenda
Sah, S.; Shah, R.; Govindan, A.; Varada, R.; Rex, K.; Varshney, U.
Utilisation of 10-formyldihydrofolate as substrate by dihydrofolate reductase (DHFR) and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) tranformylase/IMP cyclohydrolase (PurH) in Escherichia coli
Microbiology
164
982-991
2018
Escherichia coli, Escherichia coli (P15639), Escherichia coli K12 (P15639)
brenda
Boutchueng-Djidjou, M.; Collard-Simard, G.; Fortier, S.; Hebert, S.; Kelly, I.; Landry, C.; Faure, R.
The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC) plays a central role in insulin signaling and the Golgi/endosomes protein network
Mol. Cell. Proteomics
14
1079-1092
2015
Rattus norvegicus (O35567)
brenda