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Literature summary for 2.1.1.35 extracted from

  • Kealey, J.T.; Santi, D.V.
    Stereochemistry of tRNA(m5U54)-methyltransferase catalysis: 19F NMR spectroscopy of an enzyme-FUraRNA covalent complex (1995), Biochemistry, 34, 2441-2446.
    View publication on PubMed
Search for more literature for 2.1.1.35

Inhibitors

Inhibitors Comment Organism Structure
5-Fluorouracil substituted tRNA forms inhibitory stable methylated covalent complex with RUMT Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA catalytic mechanism Escherichia coli
a
S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA steric course of methyl transfer Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptors: small RNA oligomers corresponding to the T-arm of tRNA, 17-oligomer Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine in position 54 of tRNA, in the TPsiC sequence in loop IV ?
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: tRNA from E. coli Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine in position 54 of tRNA, in the TPsiC sequence in loop IV ?
S-adenosyl-L-methionine + uridine54 in tRNA methylates U54 in the TPsiC-loop of tRNA Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine in position 54 of tRNA, in the TPsiC sequence in loop IV ?

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Escherichia coli