EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.184 | A89N/F154Y |
Vmax and kcat values of the mutant enzyme are enhanced by 2.08 and 3.86fold, respectively, while the Km value decreases by 2.36fold compared to the wild type enzyme |
762304 |
| 1.1.1.184 | C227S |
displays a similar kcat, but a 30fold higher Km value for S-nitrosoglutathione, and does not show substrate inhibition |
724714 |
| 1.1.1.184 | D218V |
single nucleotide polymorphism |
740356 |
| 1.1.1.184 | D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P |
mutations introduce activity towards S-nitrosoglutathione |
724714 |
| 1.1.1.184 | DELTA31 |
deletion of the N-terminal 31 residues, kinetic parameters KM and kcat are essentially the same as those of the wild-type. It forms a tetramer in solution, which is similar to the wild-type but is less stable. Melting temperature is 48°C, which is lower than that of the wild-type (52°C) |
701097 |
| 1.1.1.184 | E142M |
increase in reaction velocity |
724831 |
| 1.1.1.184 | E142V |
increase in reaction velocity |
724831 |
| 1.1.1.184 | G135A |
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme |
-, 760516 |
| 1.1.1.184 | G180A |
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme |
-, 760516 |
| 1.1.1.184 | H68D |
produces (R)-enantiomer with low optical purity and yield |
695766 |
