Phosphoribosylformylglycinamidine synthase


In enzymology, a phosphoribosylformylglycinamidine synthase is an enzyme that catalyzes the chemical reaction
The 4 substrates of this enzyme are ATP, N2-formyl-N1-glycinamide, L-glutamine, and H2O, whereas its 4 products are ADP, phosphate, 2--N1-acetamidine, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is N2-formyl-N1-glycinamide:L-glutamine amido-ligase . Other names in common use include phosphoribosylformylglycinamidine synthetase, formylglycinamide ribonucloetide amidotransferase, phosphoribosylformylglycineamidine synthetase, FGAM synthetase, FGAR amidotransferase, 5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase, , 2-N-formyl-1-N-glycinamide:L-glutamine, and amido-ligase . This enzyme participates in purine metabolism. The results of a recent study indicate that the ERK2 signaling activated by growth and oncogenic signals leads to PFAS phosphorylation at the T619 site. In addition, ERK2-mediated PFAS phosphorylation is required for cell and tumor growth.
It is known as ADE6 in Saccharomyces cerevisiae genetics.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,, and.