2.1.1.148: thymidylate synthase (FAD)
This is an abbreviated version!
For detailed information about thymidylate synthase (FAD), go to the full flat file.
Word Map on EC 2.1.1.148
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2.1.1.148
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medicine
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tuberculosis
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dtmp
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synthases
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thymidine
-
dihydrofolate
-
maritima
-
bursaria
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2'-deoxyuridine
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paramecium
-
folate-dependent
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chlorella
-
5-substituted
-
virus-1
-
ch2h4folate
-
2'-deoxythymidine-5'-monophosphate
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flavoenzyme
-
drug development
- 2.1.1.148
- medicine
- tuberculosis
- dtmp
- synthases
- thymidine
- dihydrofolate
- maritima
- bursaria
- 2'-deoxyuridine
-
paramecium
-
folate-dependent
- chlorella
-
5-substituted
-
virus-1
-
ch2h4folate
-
2'-deoxythymidine-5'-monophosphate
-
flavoenzyme
- drug development
Reaction
Synonyms
A674R, complementing thymidylate synthase, FDTS, flavin dependent thymidylate synthase, flavin-dependent thymidylate synthase, flavin-dependent thymidylate synthase X, flavin-dependent TS, Thy1, thymidylate synthase 1, thymidylate synthase complementing protein, thymidylate synthase ThyX, thymidylate synthase X, ThyX, thyX-encoded thymidylate synthase, TSCP, TTHA1096
ECTree
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Substrates Products
Substrates Products on EC 2.1.1.148 - thymidylate synthase (FAD)
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REACTION DIAGRAM
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2
dTMP + tetrahydrofolate + FAD + H2O2
-
-
-
-
?
5,10-methylenetetrahydrofolate + BrdUMP + FADH2
?
-
-
-
?
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
dUMP binding accelerates the O2-insensitive half-reaction between NADPH and FAD by over four orders of magnitude to about 30 per s. Although dUMP does not have a direct role in FAD reduction, any turnover with molecular O2 requires its presence. Inversely, NADPH accommodation accelerates dUMP binding about 3fold and apparently precedes dUMP binding under physiological conditions. In the oxidative half-reaction, excess N5,N10-methylene-5,6,7,8-tetrahydrofolate reoxidizes FADH2 within 1 ms, thus very efficiently competing with FADH2 oxidation by O2
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
Paramecium bursaria Chlorella virus-1
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-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
dUMP dependent lag-phase for the single turnover reduction of FDTS bound FAD by NADPH
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
dTMP + tetrahydrofolate + NADP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH
dTMP + tetrahydrofolate + NADP
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
dTMP + tetrahydrofolate + NADP+
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH + H+
dTMP + tetrahydrofolate + NADP+
-
-
-
?
?
-
Paramecium bursaria Chlorella virus-1
-
oxidation of NAD(P)H is linked to the reduction of enzyme bound FAD, dUMP is required for efficient FAD reduction, omitting of 5,10-methylenetetrahydrofolate from reaction mixture increases oxidation activity by a factor of 7
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-
?
additional information
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possesses RNA-binding activity, binds to the stemloop RNA structure
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-
?
additional information
?
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possesses RNA-binding activity, binds to the stemloop RNA structure
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-
?
additional information
?
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the enzyme is essential to DNA replication
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?
additional information
?
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the enzyme is essential to DNA replication
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-
?
additional information
?
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flavin-dependent thymidylate synthase can function as an oxidase, which catalyzes the reduction of O2 to H2O2, using reduced NADPH or other reducing agents and a sequential kinetic mechanism of substrate binding. Tetrahydrofolate competitively inhibits the oxidase activity, which indicates that tetrahydrofolate and O2 compete for the same reduced and dUMP-activated enzymatic complex
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-
?
additional information
?
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an initial activation of the pyrimidine substrate by reduced flavin is required for catalysis. A H/D exchange at C5 of dUMP in D2O requires the flavin to be reduced, as observed experimentally. Chemical trapping of reaction intermediates shows the unusual intermediates of further steps
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-
?
additional information
?
-
an initial activation of the pyrimidine substrate by reduced flavin is required for catalysis. A H/D exchange at C5 of dUMP in D2O requires the flavin to be reduced, as observed experimentally. Chemical trapping of reaction intermediates shows the unusual intermediates of further steps
-
-
?
additional information
?
-
the enzyme is essential to DNA replication
-
-
?