EC Number   |
Subunits |
Reference  |
|---|
   2.1.1.220 | More |
Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate |
485272 |
| 2.1.1.220 | tetramer |
4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p) |
-, 660026 |
| 2.1.1.220 | homotetramer |
4 * 31000, SDS-PAGE |
660027 |
| 2.1.1.220 | tetramer |
the enzyme remains tetrameric upon tRNA binding, with formation of complexes involving one to two molecules of tRNA per TrmI tetramer |
699528 |
| 2.1.1.220 | heterotetramer |
dimers of tightly assembled heterodimers, formed by TrmI-6 and TrmI-61 subunits, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | More |
comparative structural analysis of TrmIs, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, and the tetramer is strengthened by four intersubunit disulfide bridges, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, interactions and structure analysis, overview |
719192 |
