2.4.2.7	D99N	mutant enzyme has very low activity	-, 724940	
2.4.2.7	E104L	site-directed mutagenesis, the mutation decreases the catalytic efficiency of the enzyme in the forward reaction	759017	
2.4.2.7	E106L	site-directed mutagenesis, decreased turnover, increased Km value for adenine and decreased Km value for 5-phosphoribose 1-phosphate compared to the wild-type	638171	
2.4.2.7	E106L	site-directed mutagenesis, the mutant shows highly reduced kcat compared to wild-type	-, 758562	
2.4.2.7	E106Q	site-directed mutagenesis, decreased turnover and Km value for 5-phosphoribose 1-phosphate compared to the wild-type	638171	
2.4.2.7	F23A	site-directed mutagenesis, the mutation on the base-binding loop severely affects the activity and efficiency of the enzyme, the mutant enzyme is about 200fold less active as compared with wild-type	-, 759176	
2.4.2.7	F25W	site-directed mutagenesis, tryptophan at the adenine binding site, kinetic constants similar to the wild-type	638167	
2.4.2.7	G108A	site-directed mutagenesis, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type	638171	
2.4.2.7	G108H	site-directed mutagenesis, decreased turnover, slightly increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type	638171	
2.4.2.7	G133D	mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient	660036