EC Number   |
Protein Variants |
Reference |
|---|
   2.4.2.6 | A15C |
is not capable of improving 2',3'-dideoxyribose transfer reaction |
705990 |
| 2.4.2.6 | A15C |
kcat is diminished as compared to wild-type |
-, 704429 |
| 2.4.2.6 | A15S |
activity with 2'-deoxycytidine and adenine as substrates is closer to that of the wild-type enzyme than that of the A15T mutant, kcat is diminished as compared to wild-type |
-, 704429 |
| 2.4.2.6 | A15S |
Ser appears a good alternative for Thr, rate of 2',3'-dideoxyribosyl transfer from 2',3'-dideoxycytidine to adenine of the two mutants is almost identical |
705990 |
| 2.4.2.6 | A15T |
a single amino-acid substitution allows the conversion of the nucleoside 2'-deoxyribosyltransferase activity to a nucleoside 2',3'-dideoxy- or 2'3'-didehydro, 2',3'-dideoxyribosyltransferase activity. Specificity for the base is unchanged compared to the wild-type. The mutant displays an improved activity to the transfer of 2',3'-dideoxyribose, which is enhanced by 250fold (depending on the donors and acceptors) while the deoxyribosyl group transfer remains acceptable (30% of the wild-type) |
705990 |
| 2.4.2.6 | A15T |
mutation allows conversion of the nucleoside 2'deoxyribosyltransferase activity to a nucleoside 2',3'-dideoxy- or 2',3'-didehydro,2',3'-dideoxyribosyltransferase activity, kcat is diminished as compared to wild-type |
-, 704429 |
| 2.4.2.6 | A15V |
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type |
-, 704429 |
| 2.4.2.6 | E105A |
site-directed mutagenesis, the mutant shows about 200fold reduced activity and a 170fold increased Km compared to the wild-type enzyme |
674900 |
| 2.4.2.6 | E98A |
catalytically inactive mutant |
638055 |
| 2.4.2.6 | E98D |
site-directed mutagenesis, molecular docking study |
759892 |
