EC Number   |
Protein Variants |
Reference |
|---|
    1.13.11.3 | R133H |
gain of function mutation confers catechol 1,2-dioxygenase activity |
-, 439509 |
| 1.13.11.3 | Y447H |
greatly reduced rate of protocatechuate oxygenation |
439508 |
| 1.13.11.3 | more |
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate |
-, 742046 |
| 1.13.11.3 | more |
immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations |
726481 |
| 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 | 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 | 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 | 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 | R142K |
like wild-type no acticity of mutated protocatechuate 3,4-dioxygenase I with 4-sulfocatechol |
439513 |
| 1.13.11.3 | more |
mutants are constructed so that their pcaG genes contained variations in repeat sequence capable of producing a selectable phenotype following a specific deletion. Deletion frequencies of the various mutations is determined and compared with repair frequencies of three different single-base mutations. |
671470 |
