Table 1.
Hydrolytic activitya of P. patens A9TLP4 (PpND)and A. thaliana NUDT3 (AtND) towards peptidase substrates.
| Substrate | Relative hydrolysis rate (%) | |
|---|---|---|
|
|
||
| PpND | AtND | |
| Arg-Arg-2NA | 100 | 100 |
| Ala-Arg-2NA | 62 | 684 |
| Ala-Ala-2NA | 40 | 366 |
| Gly-Arg-2NA | 16 | 197 |
| Pro-Arg-2NA | 14 | 622 |
| Phe-Arg-2NA | 12 | 411 |
| Asp-Arg-2NA | 0 | 0 |
| Gly-Pro-2NA | 0 | 0 |
| Gly-Phe-2NA | 0 | 0 |
| Arg-2NA | 0 | 0 |
| Leu-2NA | 0 | 0 |
| Ala-2NA | 0 | 0 |
| BANA | 0 | 0 |
a
The enzymes were incubated at 37 °C in Tris-HCl buffer (ionic strength = 0.01) pH 7.5 (PpND), respectively 7.9 (AtND) containing 75 µM CoCl2, with the substrates at a final concentration of 0.04 mM (100 % = 131.4 nmol, or 17.2 nmol of Arg2-2NA hydrolyzed per min and milligram of PpND or AtND, respectively). 2NA: 2-naphthylamide; BANA: Nα-benzoyl-L-Arg-2-naphthylamide