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Literature summary for 2.1.1.229 extracted from

  • Guy, M.P.; Phizicky, E.M.
    Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification (2014), RNA Biol., 11, 1608-1618.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

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
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?
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
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

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 ?
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?
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

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

Synonyms Comment Organism
Trm9
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Saccharomyces cerevisiae
Trm9-Trm112
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Saccharomyces cerevisiae

General Information

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