Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Structure:1ZLY_A; Human glycinamide ribonucleotide transformylase, N-terminal GART domain binds the inhibitor hydroxyacetamide ribonucleotide and the cosubstrate 10-formyl-5,8, dideazafolate (10-CHO-DDF). - View structure with Cn3D
Structure:1CDE_C, Escherichia coli glycinamide ribonucleotide transformylase, binds the substrate glycinamide ribonucleotide and a folate inhibitor. Defined at a 4A distance. - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",