EC Number   |
Protein Variants |
Reference |
|---|
   3.6.1.18 | D284A |
mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions |
-, 734615 |
| 3.6.1.18 | E169K |
site-directed mutagenesis of the probabale catalytic site residue, the Ftp_EcE169K protein variant does not show binding of FAD, inactive mutant |
757628 |
| 3.6.1.18 | E244A |
critical catalytic residue, may activate a water molecule for nucleophilic attack |
734615 |
| 3.6.1.18 | H256A |
critical catalytic residue, may neutralize the charge on the leaving group during attack |
-, 734615 |
| 3.6.1.18 | K165A |
mutation enhances the FAD diphosphatase activity |
-, 734615 |
| 3.6.1.18 | K165E |
mutation enhances the FAD diphosphatase activity |
734615 |
| 3.6.1.18 | N55Y |
complete loss of FAD hydrolyase activity, mutation converts the enzyme from an Mg2+-dependent FAD diphosphatase to an FAD-binding protein |
734615 |
| 3.6.1.18 | R245A |
critical catalytic residue, may neutralize the charge on the leaving group during attack |
734615 |
| 3.6.1.18 | S240A |
critical catalytic residue, may activate a water molecule for nucleophilic attack |
-, 734615 |
| 3.6.1.18 | T288A |
mutation in metal binding residue, abolishes FAD diphosphatase activity |
-, 734615 |
