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
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General Information
General Information on EC 2.1.1.148 - thymidylate synthase (FAD)
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physiological function
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DNA replication speed in bacteria and archaea that contain the low-activity ThyX enzyme is up to 10fold decreased compared with species that contain the catalytically more efficient ThyA, EC 2.1.1.45. Both ThyX and ThyA participate in frequent reciprocal gene replacement events. The bacterial metabolism continues to modulate the size and composition of prokaryotic genomes. The increased kinetic efficiency of thymidylate synthesis may have contributed to extending the prokaryotic evolutionary potential
physiological function
-
DNA replication speed in bacteria and archaea that contain the low-activity ThyX enzyme is up to 10fold decreased compared with species that contain the catalytically more efficient ThyA, EC 2.1.1.45. Both ThyX and ThyA participate in frequent reciprocal gene replacement events. The bacterial metabolism continues to modulate the size and composition of prokaryotic genomes. The increased kinetic efficiency of thymidylate synthesis may have contributed to extending the prokaryotic evolutionary potential