Crystallization (Comment) | Organism |
---|---|
mutant A110G. Amide nitrogen of mutants S308 shifts 0.4 A toward the catalytic site cysteine residue stabilizing the intermediate negative charge. The hydroxyl group of S308 rotates to a position where it is able to stabilize the carbanion intermediate of the acetyl-S-enzyme during its condensation with acetoacetyl-CoA | Enterococcus faecalis |
Protein Variants | Comment | Organism |
---|---|---|
A110G | overall reaction rate increases 140fold due to adjustments in the active site that result in additional stabilization of all three steps of the reaction pathway. Crystallization data | Enterococcus faecalis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterococcus faecalis | - |
- |
- |