EC Number   |
Protein Variants |
Reference |
|---|
   2.1.1.220 | D170A |
site-directed mutagenesis, mutation of a conserved active site residue |
-, 735777 |
| 2.1.1.220 | more |
mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro |
485272 |
| 2.1.1.220 | more |
siRNA knockdown of m1A58 methyltransferase subunits TRM6 or TRM61 |
721024 |
| 2.1.1.220 | more |
the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27 |
-, 758373 |
| 2.1.1.220 | more |
the reduced m1A levels observed in vivo and the lack of Mtase activity seen in vitro result from the inability of trm6-416, trm6-420, trm6-504, trm61-255 and trm6-416/trm61-255 mutants to effectively bind their tRNA substrate |
713140 |
| 2.1.1.220 | Y194A |
site-directed mutagenesis, crystallization assays of TrmI Y194A lead to poorly diffracting crystals |
-, 735777 |
| 2.1.1.220 | Y78A |
site-directed mutagenesis, mutation of a conserved active site residue. The structure of TrmI Y78A catalytic domain is unmodified regarding the binding of the SAM co-factor and the conformation of residues potentially interacting with the substrate adenine, as compared to the wild-type structure. The structure of the D170A mutant shows a flexible active site with one loop occupying in part the place of the co-factor and the second loop moving at the entrance to the active site |
-, 735777 |
