phosphoribosylaminoimidazolecarboxamide formyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.2.3 | ||||||||
CAS no. | 9032-03-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3), also known by the shorter name AICAR transformylase, is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and AICAR, whereas its two products are tetrahydrofolate and FAICAR.
This enzyme participates in purine metabolism and one carbon pool by folate.
Nomenclature
[edit]This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include:
- 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
- 5-amino-1-ribosyl-4-imidazolecarboxamide 5-phosphate,
- 5-amino-4-imidazolecarboxamide ribonucleotide transformylase,
- 5-amino-4-imidazolecarboxamide ribotide transformylase,
- 5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase,
- AICAR formyltransferase,
- AICAR transformylase,
- aminoimidazolecarboxamide ribonucleotide transformylase, and
- transformylase,
- bifunctional purine biosynthesis protein PURH,
- ATIC.
Structural studies
[edit]As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1G8M, 1M9N, 1OZ0, 1P4R, 1PKX, 1PL0, 1THZ, 2B1G, 2B1I, 2IU0, and 2IU3.
References
[edit]- HARTMAN SC, BUCHANAN JM (1959). "Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reactions". J. Biol. Chem. 234 (7): 1812–6. PMID 13672969.