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Literature summary extracted from

  • Kealey, J.T.; Lee, S.; Floss, H.G.; Santi, D.V.
    Stereochemistry of methyl transfer catalyzed by tRNA (m5U54)-methyltransferase--evidence for a single displacement mechanism (1991), Nucleic Acids Res., 19, 6465-6468.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.35 S-adenosyl-L-methionine + uridine54 in tRNA Escherichia coli tRNA modifying enzyme S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.35 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.35 S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA steric course of methyl transfer Escherichia coli
a
2.1.1.35 S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA single SN2 displacement mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.35 S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: m5U-deficient tRNA from E. coli GB1-5-39 Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA methylates 5-carbon of U in position 54 of tRNA, product is ribothymidine, which is invariant in the TPsiC loop ?
2.1.1.35 S-adenosyl-L-methionine + uridine54 in tRNA tRNA modifying enzyme Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.35 additional information
-
 assay at room temperature Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.35 S-adenosyl-L-methionine
-
 Escherichia coli