Catalytic data for the hydrolysis of PNPA catalyzed by artificial and natural zinc enzymesa.
| Entry | Catalysts | pH | pKa | k cat/Km (M−1 s−1) | TON |
|---|---|---|---|---|---|
| 1 | MINP(4a·5a + 8) | 7 | 6.2 | 194 | >474 |
| 2 | Modified TRI peptide-Zn (ref. 9) | 8 | 8.8 | 3 | >10 |
| 3 | MID1-Zn (ref. 10) | 8 | 8.2 | 180 | >50 |
| 4 | Ac-IHIHIQI-CONH2 (ref. 12) | 8 | 9.3 | 62 | >20 |
| 5 | A104AB3 (ref. 13) | 9 | 9.0 | 32 | — |
| 6 | CC-Hept–Cys–His–Glu (ref. 14) | 8 | 9.0 | 18 | >12 |
| 7 | VK2H (ref. 15) | 9 | — | 19 | — |
| 8 | Ac-IHIHIYI-NH2 at 37 °C (ref. 16) | 8 | — | 138b | — |
| 9 | F–Zn assembly18 | 7 | — | 11 | — |
| 10 | VFFAHH assembly19 | 7.4 | — | 1.7 | — |
| 11 | Human CA B20 | 7 | 7.3 | 150 | — |
| 12 | Human CA C20 | 7 | 6.8 | 1670 | — |
a
The data for the artificial zinc enzymes reported in the literature were obtained at 22–25 °C for PNPA, unless otherwise indicated.
b
The peptide assembly upon ageing becomes more active, giving a kcat/KM value of 355 M−1 s−1 after 10 days at 37 °C in a pH 8 buffer and 1 mM ZnCl2.16