EC Number   |
Protein Variants |
Reference |
|---|
   1.16.3.2 | E126A |
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein. The C-site variants (particularly E49A and E126A) fully regenerate their initial ferroxidase activity within a few hours compared to a day or so required for wild-type EcFtnA |
744322 |
| 1.16.3.2 | E126A |
the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein |
729262 |
| 1.16.3.2 | E129C |
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme |
730440 |
| 1.16.3.2 | E129Q |
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme |
730440 |
| 1.16.3.2 | E129R |
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme |
730440 |
| 1.16.3.2 | E130A |
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein |
744322 |
| 1.16.3.2 | E130A |
the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein |
729262 |
| 1.16.3.2 | E130H |
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme |
730440 |
| 1.16.3.2 | E17A |
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4 |
744322 |
| 1.16.3.2 | E17A |
the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme |
729262 |
