EC Number   |
Protein Variants |
Reference |
|---|
    1.3.98.5 | H156A |
the mutant shows less than 10% of wild type activity |
751026 |
| 1.3.98.5 | H156C |
the mutant shows less than 10% of wild type activity |
751026 |
| 1.3.98.5 | K151A |
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired |
-, 754346 |
| 1.3.98.5 | M149A |
mutation alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. In the mutant, two CO conformers are present corresponding to open (A0) and closed (A1) conformations. Residue M149 is involved in the formation of a covalent bond with a vinyl substituent of heme b at excess of hydrogen peroxide |
-, 752779 |
| 1.3.98.5 | M149A/Q187A |
binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found |
-, 752779 |
| 1.3.98.5 | Q187A |
catalytic activity similar to wild-type |
754346 |
| 1.3.98.5 | Q187A |
in the absence of the Q187, only the A0 conformer is found compared to two CO conformers are present corresponding to open (A0) and closed (A1) conformations in mutant M149A |
-, 752779 |
| 1.3.98.5 | R133A |
catalytic activity similar to wild-type |
-, 754346 |
| 1.3.98.5 | R179A |
catalytic activity similar to wild-type |
-, 754346 |
| 1.3.98.5 | Y113A |
catalytic activity similar to wild-type |
-, 754346 |
