Literature summary for 2.1.1.148 extracted from

Becker, H.F.; Djaout, K.; Lamarre, I.; Ulmer, J.E.; Schaming, D.; Balland, V.; Liebl, U.; Myllykallio, H.; Vos, M.H.
Substrate interaction dynamics and oxygen control in the active site of thymidylate synthase ThyX (2014), Biochem. J., 459, 37-45.

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Organism

Organism	UniProt	Comment	Textmining
Paramecium bursaria Chlorella virus 1	O41156	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5,10-methylenetetrahydrofolate + dUMP + FADH2	-	Paramecium bursaria Chlorella virus 1	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	?

Synonyms

Synonyms	Comment	Organism
A674R	-	Paramecium bursaria Chlorella virus 1

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Release 2023.1 (January 2023)