EC Number   |
Protein Variants |
Reference |
|---|
   2.1.1.202 | C260A |
the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA |
672512 |
| 2.1.1.202 | C260S |
the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA |
672512 |
| 2.1.1.202 | C271A |
site-directed mutagenesis, the mutant enzyme forms an irreversible covalent crosslink between itself and the methylated cytosine in its target RNA |
735907 |
| 2.1.1.202 | C310A |
the mutant shows only a slightly lower affinity for RNA compared to wild-type Trm4p. The C310A mutant of Trm4p is unable to bind RNA covalently as well as to transfer the methyl group from SAM to the RNA substrate since no activity was detectable |
710546 |
| 2.1.1.202 | C326A |
site-directed mutagenesis, tRNA binding structure compared to wild-type enzyme, the C326A mutation hampers the breakdown of the covalent intermediates |
757846 |
| 2.1.1.202 | C424A |
organism containing the C424A mutation is not viable |
639472 |
| 2.1.1.202 | C478A |
organism containing the C478A mutation is viable |
639472 |
| 2.1.1.202 | D266A |
site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity |
757846 |
| 2.1.1.202 | D293A |
site-directed mutagenesis, the mutation leads to a loss of SAM binding capability and a loss of methylation activity to tRNACys |
757846 |
| 2.1.1.202 | D323A |
site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity |
757846 |
