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
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dihydrofolate
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maritima
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bursaria
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2'-deoxyuridine
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paramecium
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folate-dependent
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chlorella
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5-substituted
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virus-1
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ch2h4folate
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2'-deoxythymidine-5'-monophosphate
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flavoenzyme
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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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Cofactor
Cofactor on EC 2.1.1.148 - thymidylate synthase (FAD)
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NADP+
expulsion of the cofactor FAD by NADP+, no anticipated ThyX-FAD-BrdUMP-NADP+ quaternary complex, but a ThyX-NADP+ binary complex
FAD
even though FAD is very well bound to three subunits, FAD interactions are not an absolute requirement for tetramer stabilization
FAD
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the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
FAD
the pro-R hydride of NADPH and not the R6 hydride of the tetrahydropterin is the reducing agent. The stereospecificity for the pro-R NADPH oxidation is not absolute. The hydride is transferred to FAD, which is the rate-limiting step of the catalytic cascade
FAD
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wild-type and mutant enzymes Y87F, S84Y, H48Q, S84A and S84C contain quantities of tightly bound FAD. Mutant enzymes R74A, R74K, H48Q/S84A and H48Q/S84C easily lose considerable amounts of bound FAD
FAD
presence of FAD additionally stabilizes the protein against thermal denaturation by 10 degrees. The assembly of thymidylate synthase with FAD is governed by a large enthalpy change opposed by an unfavorable entropy change resulting in a relatively strong nanomolar binding
FAD
presence of FAD additionally stabilizes the protein against thermal denaturation by 4.9 degrees. Binding of dUMP to FAD-loaded proteins stabilizes further. ThyX binds FAD with a low micromolar binding affinity in a process characterized by a favorable entropy change
FADH2
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the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
NADH
Paramecium bursaria Chlorella virus-1
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oxidation of NADH 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
NADPH
Paramecium bursaria Chlorella virus-1
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oxidation of NADPH 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
NADPH
the pro-R hydride of NADPH and not the R6 hydride of the tetrahydropterin is the reducing agent. The stereospecificity for the pro-R NADPH oxidation is not absolute. The hydride is transferred to FAD, which is the rate-limiting step of the catalytic cascade
NADPH
Paramecium bursaria Chlorella virus-1
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residue His53 is crucial for NADPH oxidation, is located in the vicinity of the redox active N-5 atom of the FAD ring system