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Literature summary extracted from

  • Chen, P.; Schulze-Gahmen, U.; Stura, E.A.; Inglese, J.; Johnson, D.L.; Marolewski, A.; Benkovic, S.J.; Wilson, I.A.
    Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution (1992), J. Mol. Biol., 227, 283-292.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.2.2 medicine pharmacological importance, target enzyme for chemotherapy, development of novel antifolate drugs, to be used as anti-cancer drugs Mus musculus
2.1.2.2 medicine pharmacological importance, target enzyme for chemotherapy, development of novel antifolate drugs, to be used as anti-cancer drugs Escherichia coli
2.1.2.2 medicine pharmacological importance, target enzyme for chemotherapy, development of novel antifolate drugs, to be used as anti-cancer drugs Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.2
-
 Escherichia coli
2.1.2.2 cloned by functional complementation in Escherichia coli Homo sapiens
2.1.2.2 cloning of a 12-gene cluster encoding 9 enzymes for de novo purine nucleotide synthesis Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.2 crystals grown by vapor diffusion, space group C222, a = 140.5 A, b = 98.2 A, c = 103.3 A Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.2 5,10-dideaza-5,6,7,8-tetrahydrofolate
-
 Escherichia coli
2.1.2.2 5,10-dideaza-5,6,7,8-tetrahydrofolate
-
 Homo sapiens
2.1.2.2 5,10-dideazatetrahydrofolate
-
 Escherichia coli
2.1.2.2 5,10-dideazatetrahydrofolate
-
 Homo sapiens
2.1.2.2 5,10-dideazatetrahydrofolate
-
 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.2 23000
-
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Bacillus subtilis
-
 tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Saccharomyces cerevisiae
-
 tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Drosophila melanogaster essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Mus musculus essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Escherichia coli essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide Homo sapiens essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + glycinamide ribonucleotide Mus musculus
-
 tetrahydrofolate + formylglycinamide ribonucleotide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + glycinamide ribonucleotide Escherichia coli
-
 tetrahydrofolate + formylglycinamide ribonucleotide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.2 Bacillus subtilis
-
-
-
2.1.2.2 Drosophila melanogaster
-
 fruit fly
-
2.1.2.2 Escherichia coli
-
-
-
2.1.2.2 Homo sapiens
-
 human
-
2.1.2.2 Mus musculus
-
 mouse
-
2.1.2.2 Saccharomyces cerevisiae
-
 yeast
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Drosophila melanogaster tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Bacillus subtilis tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Mus musculus tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Escherichia coli tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Homo sapiens tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
-
 Saccharomyces cerevisiae tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway Drosophila melanogaster tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway Mus musculus tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway Escherichia coli tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway Homo sapiens tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + glycinamide ribonucleotide
-
 Mus musculus tetrahydrofolate + formylglycinamide ribonucleotide
-
 ?
2.1.2.2 10-formyltetrahydrofolate + glycinamide ribonucleotide
-
 Escherichia coli tetrahydrofolate + formylglycinamide ribonucleotide
-
 ?
2.1.2.2 additional information monofunctional enzyme Bacillus subtilis ?
-
 ?
2.1.2.2 additional information monofunctional enzyme Escherichia coli ?
-
 ?
2.1.2.2 additional information 3 activities in a multifunctional protein, posessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotidetransformylase and aminoimidazole ribonucleotide synthetase Mus musculus ?
-
 ?
2.1.2.2 additional information 3 activities in a multifunctional protein, posessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotidetransformylase and aminoimidazole ribonucleotide synthetase Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.2.2 dimer
-
 Escherichia coli
2.1.2.2 dimer
-
 Saccharomyces cerevisiae