EC Number   |
Metals/Ions |
Reference |
|---|
   2.1.1.228 | Ca2+ |
can partially substitute for Mg2+ |
735927 |
| 2.1.1.228 | Ca2+ |
can substitute Mg2+ to lesser extent |
756631 |
| 2.1.1.228 | Ca2+ |
divalent cation (in oder of decreasing efficiency: Mg2+, Mn2+, Ca2+) required, optimal activity in presence of 10 mM Mg2+ |
662010 |
| 2.1.1.228 | KCl |
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl |
661154 |
| 2.1.1.228 | Mg2+ |
dependent on, one Mg2+ per enzyme dimer. Mg2+ is not involved in substrate binding, but in promoting methyl transfer. Mg2+ promotes methyl transfer of TrmD not by stabilizing the binding of tRNA or AdoMet, but by accelerating the chemical rate. Mg2+ interacts with the O6 of G37-tRNA |
735927 |
| 2.1.1.228 | Mg2+ |
divalent cation (in oder of decreasig efficiency: Mg2+, Mn2+, Ca2+) required, optimal activity in presence of 10 mM Mg2+ |
662010 |
| 2.1.1.228 | Mg2+ |
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics |
756631 |
| 2.1.1.228 | Mg2+ |
required |
736428, 756774, 757409, 757582, 757863, 758324, 758348, 758376 |
| 2.1.1.228 | Mg2+ |
required, cells expressing the native trmD show more than a 6fold activation of transcription upon switching from high to low Mg2+ media, whereas cells expressing a S88L mutant trmD show less than a 2fold activation. For cells expressing the native trmD, the level of Mg2+ modulates the level of TrmD-dependent m1G37-tRNA synthesis, which in turn modulates the speed of ribosomal translation of m1G37-dependent codons in the 5'-leader ORF. At high Mg2+, TrmD is active and the abundantly synthesized m1G37-tRNA facilitates ribosomal translation through the 5'-leader ORF |
756774 |
| 2.1.1.228 | Mg2+ |
required, one PaTrmD monomer can bind to one Mg2+ ion. Mg2+ ion does not bind tightly to PaTrmD |
758329 |
