2.4.2.17	1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes	
2.4.2.17	1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	double displacement mechanism	
2.4.2.17	1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction mechanism	
2.4.2.17	1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	substrate binding sites, active site structure, switch between active and inactive conformation