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Literature summary for 2.1.1.35 extracted from

  • Gu, X.; Ofengand, J.; Santi, D.V.
    In vitro methylation of Escherichia coli 16S rRNA by tRNA (m5U54)-methyltransferase (1994), Biochemistry, 33, 2255-2261.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
trmA gene encodes enzyme, gene is essential for the organism Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5-Fluorouracil substituted tRNA potent inhibitor Escherichia coli
tRNAPhe inhibits binding of 16S rRNA to RUMT Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme also catalyzes exchange of tritium of [3H]-Ura-16S rRNA and protons of water Escherichia coli additional information
-
?
S-adenosyl-L-methionine + 16S rRNA methyl group acceptor: E. coli 16S rRNA, site of methylation is U788 which is within a 9-base loop of a predicted stem-loop structure, mechanism is proposed to involve formation of a covalent, reversible Michael adduct with the target U788, poor substrate: methylation of 16S rRNA 40fold slower than of tRNAPhe Escherichia coli S-adenosyl-L-homocysteine + 16S rRNA containing thymine in vitro product m5U is not normally found in wild-type 16S rRNA, U788 is not highly methylated in vivo, 1 mol m5U per mol of 16S rRNA ?
S-adenosyl-L-methionine + uridine54 in tRNA substrate consensus sequence for the T-arm of tRNA consists of a 2-5 base-pair stem and a 7-base loop Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?
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
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Cofactor

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