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5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
5,10-methylenetetrahydrofolate + tRNA UpsiC + NADH
tetrahydrofolate + tRNA TpsiC + NAD+
-
-
-
-
?
5,10-methylenetetrahydrofolate + uracil54 in tRNA + FADH2
tetrahydrofolate + 5-methyluracil54 in tRNA + FAD
-
-
-
?
N5,N10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe containing ribothymidine at position 54
S-adenosyl-L-methionine + tRNAPhe mutant A58G containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58G containing ribothymidine at position 54
S-adenosyl-L-methionine + tRNAPhe mutant A58U containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58U containing ribothymidine at position 54
S-adenosyl-L-methionine + tRNAPhe mutant G57A containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant G57A containing ribothymidine at position 54
S-adenosyl-L-methionine + tRNAPhe nucleotides 18-76 containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe nucleotides 18-76 containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe nucleotides 44-76 containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe nucleotides 44-76 containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe with deletions of aminoacyl stem and D-arm containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe with deletions of aminoacyl stem and D-arm containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe with deletions of aminoacyl stem containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe with deletions of aminoacyl stem containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe with deletions of anticodon arm containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe with deletions of anticodon armand D-arm containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe with deletions of D-arm containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe with deletions of D-arm containing ribothymidine at position 54
-
-
-
?
additional information
?
-
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
TrmFO is a methyltransferase that catalyzes the formation of 5-methyluridine or ribothymidine at position 54 in tRNA in some Gram-positive bacteria
-
-
?
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
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
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
Clostridium acidi-urici
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
Treponema palladium
-
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant A58G containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58G containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant A58G containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58G containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant A58U containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58U containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant A58U containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant A58U containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant G57A containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant G57A containing ribothymidine at position 54
-
-
-
?
S-adenosyl-L-methionine + tRNAPhe mutant G57A containing uridine at position 54
S-adenosyl-L-homocysteine + tRNAPhe mutant G57A containing ribothymidine at position 54
-
-
-
?
additional information
?
-
assay method development and evaluation
-
-
?
additional information
?
-
the minimum substrate requirement exists in the T-arm structure. The positive determinants for TrmFO are the U54U55C56 sequence and G53-C61 base pair. The affinity of TrmFO for tRNA in the initial binding process is weak. The methylated tRNA is released before the structural change process. Residue A38 prevents incorrect methylation of U32 in the anticodon loop. The m1A58 modification clearly accelerates the TrmFO reaction, suggesting a synergistic effect of the 5U54,m1A58, and s2U54 modifications on 5s2U54 formation. No substrates: tRNAPhe mutants U55C, C56U, U59C, U60C, U60G, G53C/C61G, G53A/C61U, G53A/C61A, G53A, G53U, C61A, C61U
-
-
?
additional information
?
-
-
the minimum substrate requirement exists in the T-arm structure. The positive determinants for TrmFO are the U54U55C56 sequence and G53-C61 base pair. The affinity of TrmFO for tRNA in the initial binding process is weak. The methylated tRNA is released before the structural change process. Residue A38 prevents incorrect methylation of U32 in the anticodon loop. The m1A58 modification clearly accelerates the TrmFO reaction, suggesting a synergistic effect of the 5U54,m1A58, and s2U54 modifications on 5s2U54 formation. No substrates: tRNAPhe mutants U55C, C56U, U59C, U60C, U60G, G53C/C61G, G53A/C61U, G53A/C61A, G53A, G53U, C61A, C61U
-
-
?
additional information
?
-
the minimum substrate requirement exists in the T-arm structure. The positive determinants for TrmFO are the U54U55C56 sequence and G53-C61 base pair. The affinity of TrmFO for tRNA in the initial binding process is weak. The methylated tRNA is released before the structural change process. Residue A38 prevents incorrect methylation of U32 in the anticodon loop. The m1A58 modification clearly accelerates the TrmFO reaction, suggesting a synergistic effect of the 5U54,m1A58, and s2U54 modifications on 5s2U54 formation. No substrates: tRNAPhe mutants U55C, C56U, U59C, U60C, U60G, G53C/C61G, G53A/C61U, G53A/C61A, G53A, G53U, C61A, C61U
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2
tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
-
TrmFO is a methyltransferase that catalyzes the formation of 5-methyluridine or ribothymidine at position 54 in tRNA in some Gram-positive bacteria
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
-
?
5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2
tetrahydrofolate + tRNA TpsiC + FAD
-
post-transcriptional biosynthesis of ribothymidine in the tRNA
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.5
5,10-methylenetetrahydrofolate
-
-
0.0011
tRNAPhe containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0022
tRNAPhe mutant A58G containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0013
tRNAPhe mutant A58U containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0021
tRNAPhe mutant G57A containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0045
tRNAPhe nucleotides 18-76 containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0026
tRNAPhe nucleotides 44-76 containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0019
tRNAPhe with deletions of aminoacyl stem and D-arm containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0013
tRNAPhe with deletions of aminoacyl stem containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0012
tRNAPhe with deletions of anticodon arm containing uridine at position 54
pH not specified in the publication, 60°C
-
0.0015
tRNAPhe with deletions of D-arm containing uridine at position 54
pH not specified in the publication, 60°C
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Delk, A.S.; Romeo, J.M.; Nagle, D.P.; Rabinowitz, J.C.
Biosynthesis of ribothymidine in the transfer RNA of Streptococcus faecalis and Bacillus subtilis. A methylation of RNA involving 5,10-methylenetetrahydrofolate
J. Biol. Chem.
251
7649-7656
1976
Bacillus subtilis, Enterococcus faecalis, no activity in Micrococcus luteus
brenda
Delk, A.S.; Nagle, D.P.; Rabinowitz, J.C.
The methylenetetrahydrofolate-mediated biosynthesis of ribothymidine in the transfer-RNA of Streptococcus faecalis: incorporation of hydrogen from solvent into the methyl moiety
Biochem. Biophys. Res. Commun.
86
244-251
1979
Bacillus cereus, Bacillus subtilis, Enterococcus faecalis
brenda
Delk, A.S.; Nagle, D.P.; Rabinowitz, J.C.
Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2
J. Biol. Chem.
255
4387-4390
1980
Bacillus subtilis, Enterococcus faecalis
brenda
Chernyshev, A.; Fleischmann, T.; Kohen, A.
Thymidyl biosynthesis enzymes as antibiotic targets
Appl. Microbiol. Biotechnol.
74
282-289
2007
Geobacillus stearothermophilus, Bacillus anthracis, Clostridium acidi-urici, Clostridium botulinum, Mycobacterium tuberculosis, Mycobacterium leprae, Rickettsia sp., Treponema palladium
brenda
Urbonavicius, J.; Skouloubris, S.; Myllykallio, H.; Grosjean, H.
Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria -evolutionary implications
Nucleic Acids Res.
33
3955-3964
2005
Bacillus subtilis (P39815), Bacillus subtilis
brenda
Cicmil, N.
Crystallization and preliminary X-ray crystallographic characterization of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima
Acta Crystallogr. Sect. F
64
193-195
2008
Thermotoga maritima
brenda
Nishimasu, H.; Ishitani, R.; Yamashita, K.; Iwashita, C.; Hirata, A.; Hori, H.; Nureki, O.
Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase
Proc. Natl. Acad. Sci. USA
106
8180-8185
2009
Thermotoga maritima (Q9WZJ3)
brenda
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
Biochemistry
50
5208-5219
2011
Bacillus subtilis
brenda
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
J. Biol. Chem.
286
36268-36280
2011
Bacillus subtilis
brenda
Hamdane, D.; Skouloubris, S.; Myllykallio, H.; Golinelli-Pimpaneau, B.
Expression and purification of untagged and histidine-tagged folate-dependent tRNA:m5U54 methyltransferase from Bacillus subtilis
Protein Expr. Purif.
73
83-89
2010
Bacillus subtilis
brenda
Yamagami, R.; Yamashita, K.; Nishimasu, H.; Tomikawa, C.; Ochi, A.; Iwashita, C.; Hirata, A.; Ishitani, R.; Nureki, O.; Hori, H.
The tRNA recognition mechanism of folate/FAD-dependent tRNA methyltransferase (TrmFO)
J. Biol. Chem.
287
42480-42494
2012
Thermus thermophilus (Q5SID2), Thermus thermophilus, Thermus thermophilus DSM 579 (Q5SID2)
brenda
Yamagami, R.; Tomikawa, C.; Shigi, N.; Kazayama, A.; Asai, S.; Takuma, H.; Hirata, A.; Fourmy, D.; Asahara, H.; Watanabe, K.; Yoshizawa, S.; Hori, H.
Folate-/FAD-dependent tRNA methyltransferase from Thermus thermophilus regulates other modifications in tRNA at low temperatures
Genes Cells
21
740-754
2016
Thermus thermophilus (Q5SID2), Thermus thermophilus
brenda