EC Number   |
Protein Variants |
Reference |
|---|
    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 |
