Any feedback?
Literature summary for 2.1.1.225 extracted from
- Trm13p, the tRNA:Xm4 modification enzyme from Saccharomyces cerevisiae is a member of the Rossmann-fold MTase superfamily: prediction of structure and active site (2010), J. Mol. Model., 16, 599-606.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q12383 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Trm13p belongs to the RFM superfamily of MTases despite the absence of a significant sequence similarity to previously characterized members of this superfamily. The model reveals residues potentially responsible for cofactor binding, tRNA binding, and catalysis of the 2'-O-methylation reaction. The model suggests a presence of one to three disulfide bonds and/or metal ion binding site next to the substrate binding pocket | Saccharomyces cerevisiae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trm13p | - |
Saccharomyces cerevisiae |
| tRNA:Xm4 modification enzyme | - |
Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
