Table 2.
Mutants with potential to confer thermal stability or disturbance the active site of the enzyme Lacc 6.
| Alignment | Disulfide bridges | Ionic interactions | Disturbance of active site | |
|---|---|---|---|---|
| Mutant | S431D | D233C-T310C | G234R | F468P |
| I217F | H184C-S284C | S264E | F481M | |
| V79D | K396C-D399C | T147E | G420L | |
| N275K | N94C-G465C | G234K/Q271E/N270D (3-SB) | L132T | |
| N275R | D233C-T310C/H184C-S284C | G234E/Q271K/N270R | L416I | |
| V372D | D233C-T310C/H184C-S284C/ K396C-D399C (4-DB) | G234D/Q271K/N270R | L469F | |
| Q65R | D233C-T310C/H184C-S284C/K396C-D399C/N94C-G465C | G234R/Q271E/N270D (3-SB) | W85V | |
| S130D | ||||
| W85F |
Second column shows the mutations obtained by multiple alignment, these residues are highly conserved over time; in columns three to five, the mutants were build through structure-overlapping between Lacc 6 and the all other models/structures to find the conservative structures motifs. Disulfide bridges and Ionics interaccions are deposited in three and four columns, respectively. In the last column are the mutants that can break the active site.