EC Number   |
Protein Variants |
Reference |
|---|
   2.7.1.180 | E169K |
site-directed mutagenesis of the probabale catalytic site residue, the Ftp_EcE169K protein variant does not show binding of FAD, inactive mutant |
757628 |
| 2.7.1.180 | E169K |
site-directed mutagenesis, mutation of the active-site residue results in loss of FAD binding capability |
757628 |
| 2.7.1.180 | H257E |
site-directed mutagenesis, almost inactive mutant |
761498 |
| 2.7.1.180 | H257G |
site-directed mutagenesis, the mutant's flavin transfer activity is abolished. After reconstitution, the H257G shows a FAD:protein ratio nearly identical to the wild-type |
762233 |
| 2.7.1.180 | H257G |
site-directed mutagenesis, the turnover rates of His257 mutants are significantly smaller than those of wild-type ApbE, and mutants show increased Km values for both substrates, the pKa of the catalytic residue (pKES1) increases by 2 pH units in the His257 mutants compared to wild-type, the mutant shows reduced activity compared to wild-type |
761498 |
| 2.7.1.180 | H257K |
site-directed mutagenesis, almost inactive mutant |
761498 |
| 2.7.1.180 | H257T |
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type |
761498 |
| 2.7.1.180 | K207A |
site-directed mutagenesis, the mutant exhibits no detectable in vitro flavinylation activity |
757628 |
| 2.7.1.180 | more |
replacement of non-Ala residues in the positions 0, -2, -3 and -6 by Ala, and Ala-1 by Val. Keeping in mind that the position +2 is occupied by a non-typical Gln in FRD, this residue is also replaced by Ala |
761101 |
| 2.7.1.180 | Y60A |
site-directed mutagenesis, the engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity |
757628 |
