TABLE 1.
Substrate | Activity (μmol/min/mg of enzyme) | Relative activity (%) |
---|---|---|
10 mM | ||
↓ | ||
Cbz-F | 55.9 | 47 |
↓ | ||
Cbz-G-F | 119 | 100 |
↓ | ||
Cbz-G-G-F | 0.571 | 0.48 |
↓ | ||
Cbz-G | 63.0 | 53 |
↓ | ||
Cbz-R | 0.014 | 0.01 |
↓ | ||
G-F | 107b | 90 |
↓ | ||
G-G-F | 1.21b | 1.0 |
↓ | ||
G-G-G-F | 0.551b | 0.46 |
↓ | ||
Ac-G-F | 105a | 88 |
↓ | ||
Ac-G-G-F | 0.773b | 0.65 |
↓ | ||
Ac-G-G-G-F | 0.48b | 0.40 |
5 mM | ||
↓ | ||
Ac-M | 38.1 | 43 |
↓ | ||
Ac-Y | 37.3 | 29 |
↓ | ||
Ac-F | 24.9 | 27 |
↓ | ||
Ac-A | 10.5 | 15 |
↓ | ||
Ac-W | 1.99 | 2.7 |
↓ | ||
Ac-G | 7.40 | 2.1 |
The hydrolytic reaction was carried out at 85°C in 50 mM phosphate buffer (pH 7.5) containing 5% DMF. The cleavage site for the substrate is shown by the arrow.
The hydrolytic activity (release of F) was measured by HPLC.