EC Number   |
Protein Variants |
Reference |
|---|
   1.13.11.38 | A85H |
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected. |
-, 725836 |
| 1.13.11.38 | L38Q |
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme |
-, 725836 |
| 1.13.11.38 | more |
generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview |
-, 725836 |
| 1.13.11.38 | W104Y |
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates |
-, 725836 |
