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Literature summary for 2.1.1.74 extracted from

  • Hamdane, D.; Argentini, M.; Cornu, D.; Myllykallio, H.; Skouloubris, S.; Hui-Bon-Hoa, G.; Golinelli-Pimpaneau, B.
    Insights into folate/FAD-dependent tRNA methyltransferase mechanism: role of two highly conserved cysteines in catalysis (2011), J. Biol. Chem., 286, 36268-36280.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.74

Protein Variants

Protein Variants Comment Organism
C193A mutant is nearly as active as the wild-type enzyme Bacillus subtilis
C226A mutant loses both the tRNA methylation activity and the capacity to form a covalent complex with the 5-FU-mini-RNA Bacillus subtilis
C53A mutant is inactive but like the wild-type enzyme, mutant C53A is capable of forming a covalent complex with a 5-fluorouridine-containing mini-RNA. Mutation of Cys-53 changes the accessibility of the FAD-binding site and impairs the conformational stability of TrmFO Bacillus subtilis
C53A/C226A as for the single C226A mutant, no protein-RNA covalent complex is detectable with the double mutant Bacillus subtilis
S54A mutant is nearly as active as the wild-type enzyme Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
folate-dependent tRNA methyltransferase
-
 Bacillus subtilis
TRMFO
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis