Table 2. Relative hydrolase activity of recombinant wild-type and mutant Endo-CC1s.
| Endo-CC1 | Relative activity (%) a |
|---|---|
| WT (N180) | 100 |
| A | 0.5 |
| C | 2.1 |
| D | 5.8 |
| E | 3.3 |
| F | 0.1 |
| G | 0.4 |
| H | 8.7 |
| I | 4.0 |
| K | 0.2 |
| L | 0.6 |
| M | 12.0 |
| P | 0.8 |
| Q | 16.9 |
| R | ND b |
| S | 1.0 |
| T | 1.0 |
| V | 3.4 |
| W | ND b |
| Y | ND b |
The Asn 180 (N180) residue of the wild-type (WT) Endo-CC1 was replaced individually with the one of the remaining 19 amino acid residues (indicated above using single-letter code for each amino acid residue) and the relative hydrolase activity of each mutant was determined using purified recombinant mutant and Dns-DG as the substrate.
a The relative activity of the WT Endo-CC1 was set as 100.
b ND, not detectable.