TABLE 2 .
Activities of LytA point mutants in the turbidity lysis assay
| Mutation(s) | Activitya | Function or positionb |
|---|---|---|
| None (wt-LytA) | ***** | |
| H24A | − | Buried |
| H26A | − | Zinc ligand |
| H54A | − | Buried |
| E87A | − | Catalytic |
| H133A | − | Zinc ligand |
| D149A | − | Zinc ligand |
| S33Q | * | β-Region |
| Y41A/R | * | β-Region |
| K131A | * | Buried |
| H147A/K | * | Catalytic |
| N30L/Q | *** | β-Region |
| R44E/Q | *** | β-Region |
| W72A | *** | γ-Region |
| G75A | *** | γ-Region |
| N79A | *** | γ-Region |
| V148E/K | *** | α-Region |
| G29A | **** | α-Region |
| S33A | **** | β-Region |
| C60R | **** | Peripheral |
| S91A | **** | Peripheral |
| K45R | ***** | Branch point |
| F52A/V | ***** | β-Region |
| C60A/E | ***** | Peripheral |
| C60A + C136A | ***** | Peripheral + buried |
| C136A | ***** | Buried |
| T137A | ***** | Peripheral |
| N142A | ***** | Peripheral |
| H144A | ***** | γ-Region |
| S145A | ***** | Branch point |
| H166A | ***** | Peripheral |
a
The relative enzymatic activities of LytA protein variants are given in the following intervals: *****, 100 to 80%; ****, 79 to 60%; ***, 59 to 40%; **, 39 to 20%; *, 19 to 5%; −, 4 to 0%.
b
Buried residues are part of the hydrophobic core, and peripheral residues are surface-exposed residues outside the binding crevice. Zinc ligand and catalytic residues form the catalytic center. Branch point residues and α-, β-, and γ-regions represent subregions of the binding crevice.