EC Number   |
Protein Variants |
Reference |
|---|
    1.13.11.3 | Y408C |
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly. |
671966 |
| 1.13.11.3 | Y408C |
turnover-number is 523fold lower than that of the wild-type enzyme |
657551 |
| 1.13.11.3 | Y408E |
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. |
671966 |
| 1.13.11.3 | Y408E |
turnover-number is 6800fold lower than that of the wild-type enzyme |
657551 |
| 1.13.11.3 | Y408F |
iron is not tightly bound, the Y408F mutant does not reconstitute above half-occupancy and loses color during crystallization attempts. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly. |
671966 |
| 1.13.11.3 | Y408H |
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly. |
671966 |
| 1.13.11.3 | Y408H |
turnover-number is 9714fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 10fold lower than that of the wild-type enzyme |
657551 |
| 1.13.11.3 | Y447H |
greatly reduced rate of protocatechuate oxygenation |
439508 |
| 1.13.11.3 | Y447H |
turnover-number is 567fold lower than that of the wild-type enzyme |
657551 |
