Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + carboxymethyl-2-thiouridine34 in tRNA | Saccharomyces cerevisiae | Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis | S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)-2-thiouridine34 in tRNA | - |
? | |
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA | Saccharomyces cerevisiae | Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis | S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | recombinant tagged Sc Trm9 protein purified from yeast methylates a saponified tRNA extract, demonstrating that Sc Trm9 is required for formation of the terminal methyl group of mcm5U | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + carboxymethyl-2-thiouridine34 in tRNA | Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)-2-thiouridine34 in tRNA | - |
? | |
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA | Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | the enzyme is formed by catalytic subunit Trm9 and regulatory subunit Trm112 | Saccharomyces cerevisiae |
More | different catalytic subunits engage the same partner protein Trm112 to direct different chemical modifications on different residues | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Trm9 | - |
Saccharomyces cerevisiae |
Trm9-Trm112 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
evolution | the mcm5U family of modifications is found only in eukaryotes and is implicated in efficient reading of AGA and AAG codons by tRNAArg (UCU) and tRNAGlu(UUC), respectively in Saccharomyyces cerevisiae. Trm112 partners with several methyltransferases involved in diverse translational processes and has distinct roles in other methyltransferase complexes | Saccharomyces cerevisiae |
malfunction | Trm9DELTA mutation causes lack of the 5-methoxycarbonylmethyluridine (mcm5U34) modification in yeast which is associated with sensitivity to DNA damaging agents as well as with sensitivity to aminoglycosides at high temperature and resistance to zymocin-mediated tRNA cleavage and cell death. Mutants encoding Sc Trm9 variants lacking the C-terminal domain required for interaction with Sc Trm112 act as suppressors of zymocin toxicity | Saccharomyces cerevisiae |
additional information | different catalytic subunits, e.g. Trm9, engage the same partner protein Trm112 to direct different chemical modifications on different residues | Saccharomyces cerevisiae |