EC Number   |
General Information |
Reference |
|---|
   2.1.1.229 | malfunction |
5-methoxycarbonylmethyl-uridine or 5-methoxycarbonylmethyl-2-thiouridine are absent in tRNAs in trm9DELTA or trm112DELTA mutants, while intermediates 5-carbamoylmethyluridine and 5-methoxycarbonylmethyl-2-thiouridine are accumulating |
720827 |
| 2.1.1.229 | malfunction |
ABH8 depletion in human cells reduces endogenous levels of 5-methoxycarboxymethyluridine in RNA and increases cellular sensitivity to DNA-damaging agents |
713017 |
| 2.1.1.229 | physiological function |
ALKBH8 is an upstream target of NOX-1 and is involved in intracellular ROS generation. ALKBH8/NOX-1 signals function mainly in the acquisition of the aggressive human urothelial carcinoma phenotype |
711667 |
| 2.1.1.229 | physiological function |
ALKBH8-mediated methylation is a prerequisite for the thiolation and 2'-O-ribose methylation that form 5-methoxycarbonylmethyl-2-thiouridine and 5-methoxycarbonylmethyl-2'-O-methyluridine, respectively |
713016 |
| 2.1.1.229 | physiological function |
at position 34, the majority of yeast cytosolic tRNA species that have a uridine are modified to 5-carbamoylmethyluridine, 5-carbamoylmethyl-2'-O-methyluridine, 5-methoxycarbonylmethyl-uridine or 5-methoxycarbonylmethyl-2-thiouridine. The formation of 5-methoxycarbonylmethyl-uridine and 5-carbamoylmethyluridine side chains involves a complex pathway, where the last step in formation of mcm5 is a methyl esterification of 5-carboxymethyl dependent on the Trm9 and Trm112 proteins. Both Trm9 and Trm112 are required for the last step in formation of 5-methoxycarbonylmethyl side chains at wobble uridines |
720827 |
| 2.1.1.229 | evolution |
comparison of the MnmC2 active sites between Escherichia coli MnmC and Yersinia pestis MnmC, overview. Structural comparison with MnmC2 of Aquifex aeolicus |
-, 735868, 735869 |
| 2.1.1.229 | evolution |
conservation of Arg199, the key residue of CmoA that stabilizes the negative charge of the carboxyl group of the S-adenosyl-S-carboxymethyl-L-homocysteine cofactor, suggests that these proteins contain the S-adenosyl-S-carboxymethyl-L-homocysteine cofactor instead of S-adenosyl-L-methionine. The equivalent residue in known S-adenosyl-L-methionine-dependent methyltransferases is not conserved |
735357 |
| 2.1.1.229 | more |
crystal structure of MnmC from the Gram negative bacterium reveals the overall architecture of the enzyme and the relative disposition of the two independent catalytic domains: a Rossmann-fold domain containing the S-adenosyl-L-methionine binding site and an FAD containing domain structurally homologous to glycine oxidase from Bacillus subtilis. The structure of MnmC also reveals the detailed atomic interactions at the interdomain interface and provide spatial restraints relevant to the overall catalytic mechanism |
735868 |
| 2.1.1.229 | more |
crystal structures of MnmC from two Gram negative bacteria reveal the overall architecture of the enzyme and the relative disposition of the two independent catalytic domains: a Rossmann-fold domain containing the S-adenosyl-L-methionine binding site and an FAD containing domain structurally homologous to glycine oxidase from Bacillus subtilis. The structures of MnmC also reveal the detailed atomic interactions at the interdomain interface and provide spatial restraints relevant to the overall catalytic mechanism |
-, 735869 |
| 2.1.1.229 | more |
different catalytic subunits, e.g. Trm9, engage the same partner protein Trm112 to direct different chemical modifications on different residues |
737223 |
