EC Number   |
General Information |
Reference |
|---|
   2.1.1.296 | evolution |
MT57 homologs are only found in trypanosomatid protozoa that have a cap 4 structure and in poxviruses, of which vaccinia virus is a prototype, TbMT48 or TbMT57 are two protein components of the cap 4 biosynthetic machinery |
677099 |
| 2.1.1.296 | evolution |
the enzyme belongs to the Rossmann-fold MTase (RFM) family, hMTr1 and hMTr2 are paralogues forming a subfamily with higher eukaryotic and viral members, minimum evolution tree of homologues of known 2'-O-ribose mRNA cap MTases, overview |
728390 |
| 2.1.1.296 | evolution |
the enzyme shows significant sequence and structural similarities to vaccinia virus VP39, another cap-specific RNA 2'-O-methyltransferase. TbMT48 or TbMT57 are two protein components of the cap 4 biosynthetic machinery |
728268 |
| 2.1.1.296 | malfunction |
an observed defect in cap 4 modification is a specific effect of MT48 ablation |
728268 |
| 2.1.1.296 | malfunction |
downregulation by RNAi or genetic ablation of TbMT57 result in the accumulation of SL RNA missing 2'-O-methyl groups at positions +3 and +4 and thus bearing a cap 2 rather than a cap 4. Genetic ablation of MT57 results in viable cells with no apparent defect in SL RNA transsplicing, suggesting that MT57 is not essential or that trypanosomes have developed alternate mechanisms to counteract the absence of this protein |
677099 |
| 2.1.1.296 | malfunction |
the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity |
736863 |
| 2.1.1.296 | metabolism |
the 5' cap of human messenger RNA contains 2'-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Enzyme responsible for the methylations are CMTr1 and CMTr2, respectively |
736863 |
| 2.1.1.296 | more |
enzyme MT48 structural modeling using the VP39 crystal structure as a template, TbMT48 domains involved in S-adenosyl-methionine and cap binding, overview |
728268 |
| 2.1.1.296 | more |
FTSJD1, the candidate hMTr2, is composed of two RFM domains, sequence comparisons, and has a K-D-K active site. Each residue of the K-D-K triad is essential for the activity of the enzyme |
728390 |
| 2.1.1.296 | more |
structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation, homology modeling of the CMTr2 catalytic domain bound to its target using the crystal structure of CMTr1 catalytic domain, overview. CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation. Residues K74, L77, W85, T89, K307, H142, and E145 are involved in RNA binding and catalysis, while residues residues S78, H86 and Q113 are not important |
736863 |
