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Literature summary extracted from

  • Baggott, J.E.; Tamura, T.
    Evidence for the hypothesis that 10-formyldihydrofolate is the in vivo substrate for aminoimidazolecarboxamide ribotide transformylase (2010), Exp. Biol. Med. (Maywood), 235, 271-277.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.3 additional information methotrexate, MTX, cannot directly inhibit AICAR transformylase, but blocks the AICAR transformylase process in patients with rheumatoid arthritis Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.3 additional information
-
 additional information 10-formyl-7,8-dihydrofolate has an about 5fold kinetic advantage, Vm/Km, over 10-formyl-5,6,7,8-tetrahydrofolate for AICAR transformylases in human leukemia cells and for human recombinant AICAR transformylase Homo sapiens
2.1.2.3 additional information
-
 additional information 10-formyl-7,8-dihydrofolate has an about 5fold kinetic advantage, Vm/Km, over 10-formyl-5,6,7,8-tetrahydrofolate for AICAR transformylases in rat bone marrow cells Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.2.3 cytoplasm AICAR transformylase does not form clusters Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Homo sapiens 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Rattus norvegicus 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 additional information Homo sapiens 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 ?
-
 ?
2.1.2.3 additional information Rattus norvegicus 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.3 Homo sapiens
-
-
-
2.1.2.3 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.2.3 bone marrow cell
-
 Rattus norvegicus
-
2.1.2.3 carcinoma cell
-
 Homo sapiens
-
2.1.2.3 leukemia cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase Homo sapiens dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 10-formyl-7,8-dihydrofolate is the in vivo substrate for AICAR transformylase Rattus norvegicus dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-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 Homo sapiens dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyl-7,8-dihydrofolate + 5-amino-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 Rattus norvegicus dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 Homo sapiens tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 Rattus norvegicus tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 r
2.1.2.3 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 Homo sapiens ?
-
 ?
2.1.2.3 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 Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.3 AICAR transformylase
-
 Homo sapiens
2.1.2.3 AICAR transformylase
-
 Rattus norvegicus
2.1.2.3 aminoimidazolecarboxamide ribotide transformylase
-
 Homo sapiens
2.1.2.3 aminoimidazolecarboxamide ribotide transformylase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.3 N10-formyl-7,8-dihydrofolate kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylase Homo sapiens
2.1.2.3 N10-formyl-7,8-dihydrofolate kinetically preferred over 10-formyl-5,6,7,8-tetrahydrofolate by AICAR transformylase Rattus norvegicus

General Information

EC Number General Information Comment Organism
2.1.2.3 metabolism aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis Rattus norvegicus
2.1.2.3 metabolism aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis. No enzyme complex that generates 10-formyl-5,6,7,8-tetrahydrofolate and immediately channels or furnishes it to AICAR transformylase is needed because the first oxidation product of 10-formyl-5,6,7,8-tetrahydrofolate is 10-formyl-7,8-dihydrofolate that is utilized by this transformylase Homo sapiens
2.1.2.3 additional information structure and active site of AICAR transformylase are not consistent with other enzymes that utilize 10-formyl-5,6,7,8-tetrahydrofolate. Methotrexate blockage of the AICAR transformylase process in patients with rheumatoid arthritis suggests that dihydrofolate reductase is involved and is consistent with dihydrofolate and 10-formyl-7,8-dihydrofolate being the product and substrate for AICAR transformylase Homo sapiens
2.1.2.3 additional information structure and active site of AICAR transformylase are not consistent with other enzymes that utilize 10-formyl-5,6,7,8-tetrahydrofolate. Methotrexate blockage of the AICAR transformylase process in patients with rheumatoid arthritis suggests that dihydrofolate reductase is involved and is consistent with dihydrofolate and 10-formyl-7,8-dihydrofolate being the product and substrate for AICAR transformylase Rattus norvegicus
2.1.2.3 physiological function 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase, an enzyme in purine nucleotide biosynthesis de novo, which introduces C2 into the purine ring Homo sapiens
2.1.2.3 physiological function 10-formyl-7,8-dihydrofolate, not 10-formyl-5,6,7,8-tetrahydrofolate, is the predominant in vivo substrate for mammalian aminoimidazolecarboxamide ribotide transformylase, an enzyme in purine nucleotide biosynthesis de novo, which introduces C2 into the purine ring Rattus norvegicus