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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]

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C193A
-
mutant is nearly as active as the wild-type enzyme
C226A
-
mutant loses both the tRNA methylation activity and the capacity to form a covalent complex with the 5-FU-mini-RNA
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
C53A/C226A
-
as for the single C226A mutant, no protein-RNA covalent complex is detectable with the double mutant
R312G
-
mutant isolated after cloning is found to be defective in tRNA methylation, with an activity corresponding only to 40% that of the wild-type enzyme
S54A
-
mutant is nearly as active as the wild-type enzyme
C223A
site-directed mutagenesis, almost inactive mutant
C51A
site-directed mutagenesis, almost inactive mutant
E341A
site-directed mutagenesis, the active mutant shows a decrease in both FAD binding and methylation activity compared to the wild-type enzyme
H308A
site-directed mutagenesis, the mutant shows 57% of wild-type enzyme activity compared to the wild-type enzyme
K282A
site-directed mutagenesis, almost inactive mutant
K287A
site-directed mutagenesis, almost inactive mutant
K409A
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
K410A
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
N310A
site-directed mutagenesis, the mutant shows 23% of wild-type enzyme activity compared to the wild-type enzyme
R97A
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
W283A
site-directed mutagenesis, the mutant shows slightly decreased activity