EC Number   |
Protein Variants |
Reference |
|---|
    1.13.11.49 | more |
a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions |
-, 725529 |
| 1.13.11.49 | Q74E |
the catalytic efficiency (kcat/KM) of chlorite degradation of the variant is similar to that of the wild type protein |
764186 |
| 1.13.11.49 | Q74V |
the catalytic efficiency (kcat/KM) of chlorite degradation of the variant is similar to that of the wild type protein |
764186 |
| 1.13.11.49 | R173A |
leakage of hypochlorite during the reaction is higher than that in the wild-type protein |
741901 |
| 1.13.11.49 | R173A |
mutation increases the extent of irreversible inactivation. In the presence of the hypochlorite traps methionine, monochlorodimedone, and 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]benzoic acid, the extent of chlorite degradation and release of molecular oxygen is significantly increased, whereas heme bleaching and oxidative modifications of the protein are suppressed |
741895 |
| 1.13.11.49 | R173A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme |
712897 |
| 1.13.11.49 | R173K |
mutation increases the extent of irreversible inactivation. In the presence of the hypochlorite traps methionine, monochlorodimedone, and 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]benzoic acid, the extent of chlorite degradation and release of molecular oxygen is significantly increased, whereas heme bleaching and oxidative modifications of the protein are suppressed |
741895 |
| 1.13.11.49 | R173K |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme |
712897 |
| 1.13.11.49 | R183a |
the mutation results in the loss of the ability to bind acetate |
765093 |
| 1.13.11.49 | R183Q |
mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F- |
-, 741941 |
