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Literature summary extracted from

  • Hamdane, D.; Guerineau, V.; Un, S.; Golinelli-Pimpaneau, B.
    A catalytic intermediate and several flavin redox states stabilized by folate-dependent tRNA methyltransferase from Bacillus subtilis (2011), Biochemistry, 50, 5208-5219.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.74 expressed in Escherichia coli as a His-tagged fusion protein Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.74 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.74 using Ni-NTA chromatography Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.74 5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
-
Bacillus subtilis tetrahydrofolate + tRNA TpsiC + FAD
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.74 folate-dependent tRNA methyltransferase
-
Bacillus subtilis
2.1.1.74 TRMFO
-
Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.74 37
-
assay at Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.74 7.5
-
assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.74 FADH2 using spectroscopic characterization it is shown that TrmFO stabilizes the protonated semiquinone FADH and a catalytic intermediate containing most likely both methylenetetrahydrofolate and an FAD reduced form. TrmFO, in the absence of tRNA, maintains an insulated active site that locks up the methyl donor and protects the reduced forms of the flavin from deleterious oxidative reactions Bacillus subtilis