Table 2.
Phosphorolytic activity of recombinant enzymes on natural nucleosidesa
| Substrate | Mean phosphorolytic activity (%) ± SD |
||||
|---|---|---|---|---|---|
| TTC0188 | TTC0194 | TTC1070 | TTC1412 | TTC1491 | |
| Adenosine | ND | 24.2 ± 0.2 | ND | ND | ND |
| 2′-Deoxyadenosine | ND | 27.8 ± 0.4 | ND | ND | ND |
| Guanosine | ND | ND | 8.7 ± 0.1 | ND | ND |
| 2′-Deoxyguanosine | ND | ND | 22.5 ± 0.3 | ND | ND |
| Inosine | ND | ND | 19.1 ± 0.2 | ND | ND |
| 2′-Deoxyinosine | ND | ND | 40.5 ± 0.3 | ND | ND |
| Uridine | ND | ND | ND | 15.2 ± 0.5 | ND |
| 2′-Deoxyuridine | ND | ND | ND | 40.0 ± 1.2 | ND |
| Thymidine | ND | ND | ND | 29.7 ± 0.9 | ND |
| Cytidine | ND | ND | ND | ND | ND |
| 2′-Cytidine | ND | ND | ND | ND | ND |
a
Reaction conditions: 5 mM nucleoside in sodium phosphate buffer (50 mM, pH 7.0), 5 μg of enzyme extract ml−1. Reactions were performed for 30 min at 65°C and stopped in 1 volume of ice-cold methanol. The activities are expressed as a percentage of phosphorolyzed nucleoside with respect to the total amount of nucleoside used as a substrate. ND, not detected.