EC Number   |
General Information |
Reference |
|---|
  2.1.1.205 | evolution |
sequence and structure-function comaprisons of yeast Trm7 and Trm7 enzymes from other species. Trm7 has the class I-type Rossmann fold, frequently found in SAM-dependent RNA methyltransferases, and probably employs a 2'-O-methylation mechanism similar to that of Escherichia coli RlmE, given that their overall structures are similar and that catalytic residues and SAM-binding mode are highly conserved |
-, 757855 |
| 2.1.1.205 | malfunction |
a trm7DELTA strain, which is viable but grows slowly, translation is impaired. Protein synthesis is reduced to 30% in the deleted strain, compared with an isogenic wild-type strain. The formation of 2'-O-methylcytidine32 and guanosine34 is abolished in the trm7DELTA strain |
708328 |
| 2.1.1.205 | metabolism |
the degree of some of the modifications in tRNAs from Saccharomyces cerevisiae may be regulated by the balance between substrate tRNAs and modification enzymes. Because one of key modifications, Cm32, is conferred by Trm7-Trm732, it is clear that the activity of Trm7-Trm734 is regulated by the quantitative balance between Trm732 and Trm734 |
-, 757855 |
| 2.1.1.205 | more |
the structure of tRNA methyltransferase complex of Trm7 and Trm734 (regulator of Ty1 transposition protein 10, RTT10, UniProt Q08924) reveals another binding interface for tRNA recognition, crystal structure analysis and substrate tRNA recognition by Trm7-Trm734, and active site structure, overview. Hydrogen bonds and salt bridges between Trm7 and Trm734 are determined |
-, 757855 |
