EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.1.1.228 | more |
guanosine37-methylation by TRM5 occurs regardless of the nature of the nucleotide at position 36. TRM5 also methylates inosine at position 37. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity. The enzyme does not methylate adenosine37, cytosine37 or uridine37 in tRNA. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity |
Homo sapiens |
? |
- |
? |
| 2.1.1.228 | more |
no activity with guanine37 in yeast tRNAAsp(GUC) possessing a C36G37 sequence, guanine37 in Haloferax volcanii tRNAGlu(UUC) possessing a C36G37 sequence, guanine37 in yeast tRNAPhe A36U mutant(GAU) possessing a U36G37 sequence, guanine37 in Escherichia coli tRNASer(UGA) possessing a A36G37 sequence |
Aquifex aeolicus |
? |
- |
? |
| 2.1.1.228 | more |
the enzyme is specific for methylation of guanine37 in tRNA. No methylation of tRNAArg(UCU) possessing the sequence U36G37 |
Methanocaldococcus jannaschii |
? |
- |
? |
| 2.1.1.228 | more |
TrmD recognizes the G36pG37 motif preferentially and does not methylate inosine. The TrmD enzyme is tolerant of alterations in tRNA-protein tertiary interactions as long as the core tRNA structure and the G36pG37 are present |
Escherichia coli |
? |
- |
? |
| 2.1.1.228 | more |
Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon |
Methanocaldococcus jannaschii |
? |
- |
? |
| 2.1.1.228 | more |
TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon |
Escherichia coli |
? |
- |
? |
| 2.1.1.228 | more |
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, Trm5 shows a less rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in MjtRNACys, to design the optimal substrate for Trm5 |
Methanocaldococcus jannaschii |
? |
- |
? |
| 2.1.1.228 | more |
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, TrmD shows a more rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in EctRNALeu, to design the optimal substrate for TrmD. All but deoxyG of these analogs probed the Watson-Crick basepairing interface of G37 |
Escherichia coli |
? |
- |
? |
| 2.1.1.228 | more |
structure of Trm5 active site bound to tRNA and S-adenosyl-L-methionine, induced fit for active-site assembly, detailed overview. E185 is crucial both for general base catalysis and for the conformational change that precedes catalysis |
Methanocaldococcus jannaschii |
? |
- |
? |
| 2.1.1.228 | more |
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively) |
Pyrococcus abyssi |
? |
- |
- |
