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Literature summary extracted from

  • Nishimasu, H.; Ishitani, R.; Yamashita, K.; Iwashita, C.; Hirata, A.; Hori, H.; Nureki, O.
    Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase (2009), Proc. Natl. Acad. Sci. USA, 106, 8180-8185.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.74 expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.74 free TrmFO or bound to tetrahydrofolate-bound or glutathione, addition of GSH greatly improves the quality of the crystals, X-ray diffraction structure determinationand analysis at 2.1 A, 1.6 A, and 1.05 A resolutions, respectively Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.74 C223A site-directed mutagenesis, almost inactive mutant Thermotoga maritima
2.1.1.74 C51A site-directed mutagenesis, almost inactive mutant Thermotoga maritima
2.1.1.74 E341A site-directed mutagenesis, the active mutant shows a decrease in both FAD binding and methylation activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 H308A site-directed mutagenesis, the mutant shows 57% of wild-type enzyme activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 K282A site-directed mutagenesis, almost inactive mutant Thermotoga maritima
2.1.1.74 K287A site-directed mutagenesis, almost inactive mutant Thermotoga maritima
2.1.1.74 K409A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 K410A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 N310A site-directed mutagenesis, the mutant shows 23% of wild-type enzyme activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 R97A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Thermotoga maritima
2.1.1.74 W283A site-directed mutagenesis, the mutant shows slightly decreased activity Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.74 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 Thermotoga maritima
-
 tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.74 Thermotoga maritima Q9WZJ3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.74 recombinant enzyme from Escherichia coli to homogeneity Thermotoga maritima

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.74 5,10-methylenetetrahydrofolate + uracil54 in tRNA + NAD(P)H + H+ = tetrahydrofolate + 5-methyluracil54 in tRNA + NAD(P)+ catalytic mechanism and active site structure, the methylene of MTHF is directly transferred onto U54, and then the exocyclic methylene of U54 is reduced by FADH2, overview Thermotoga maritima
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.74 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
-
 Thermotoga maritima tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
 ?
2.1.1.74 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 tetrahydrofolate is sandwiched between the flavin ring of FAD and the imidazole ring of a His residue, the transferring methylene group of MTHF is located close to the redox-active N5 atom of FAD, TrmFO-tRNA docking model and active site structure, overview Thermotoga maritima tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
 ?
2.1.1.74 additional information assay method development and evaluation Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.74 folate/FAD-dependent tRNA T54 methyltransferase
-
 Thermotoga maritima
2.1.1.74 TRMFO
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.74 60
-
 assay at Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.74 FAD dependent on, recognition and binding structure, overview Thermotoga maritima