The irreversible transfer of a formyl group to cytosolic 5-phosphoribosylglycinamide (GAR) to form 5'-phosphoribosylformylglycinamide (FGAR) is catalyzed by the phosphoribosylglycinamide formyltransferase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990; Zhang et al. 2002). Fluoresence microscopy studies of cultured human cells have shown that GART is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).
|GART||phosphoribosylglycinamide formyltransferase activity (0004644)|
|2147474||De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli||Nucleic Acids Res||1990|
|12450384||Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR||Biochemistry||2002|
|11381136||Localization of GAR transformylase in Escherichia coli and mammalian cells||Proc Natl Acad Sci USA||2001|
|18388293||Reversible compartmentalization of de novo purine biosynthetic complexes in living cells||Science||2008|