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Literature summary for 2.1.1.35 extracted from

  • Shugart, L.; Chastain, B.
    Escherichia coli tRNA (uracil-5-)-methyltransferase: Inhibition by analogues of adenosylhomocysteine (1979), Enzyme, 24, 353-357.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-homocysteine product inhibition, competitive to S-adenosyl-L-methionine Escherichia coli
structural analogues of S-adenosyl-L-homocysteine inhibition competitive to S-adenosyl-L-methionine Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uridine54 in tRNA S-adenosyl-L-methionine/S-adenosyl-L-homocysteine binding site, terminal NH2-group of the amino acid moiety is nessecary for activity Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?

Cofactor

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