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2.1.1.74: methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing]

This is an abbreviated version!
For detailed information about methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing], go to the full flat file.

Word Map on EC 2.1.1.74

Reaction

5,10-methylenetetrahydrofolate
+
uracil54 in tRNA
+
NAD(P)H
+
H+
=
tetrahydrofolate
+
5-methyluracil54 in tRNA
+
NAD(P)+

Synonyms

EC 2.1.2.12, FDRTS, folate-dependent ribothymidyl synthase, folate-dependent tRNA methyltransferase, folate/FAD-dependent tRNA T54 methyltransferase, methylenetetrahydrofolate-transfer ribonucleate uracil 5-methyltransferase,, TRMFO, tRNA (m5U54)-methyltransferase, tRNA:m5U-54 MTase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.74 methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing]

Crystallization

Crystallization on EC 2.1.1.74 - methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing]

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
purified recombinant enzyme, from 25% v/v PEG 4000, 100 mM NaCl and sodium citrate buffer, pH 5.0, at 291 K using the hanging-drop vapor-diffusion method in 0.0016 ml with 8 mg/ml protein, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution
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