Literature summary extracted from

Chernyshev, A.; Fleischmann, T.; Koehn, E.M.; Lesley, S.A.; Kohen, A.
The relationships between oxidase and synthase activities of flavin dependent thymidylate synthase (FDTS) (2007), Chem. Commun. (Camb. ), 19, 2861-2863.

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.45	Thermotoga maritima	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.1.1.45	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP	O2 and methylenetetrahydrofolate compete for the reduced enzyme after dUMP binding. dUMP enhances the rate of the oxidative half reaction and while the oxidase reaction is faster than the reaction with methylenetetrahydrofolate, this cofactor slows down the consumption of NADPH in the presence of O2 in accordance with substrate competition. dUMP, the substrate of the oxidative half reaction does not affect the reductive half reaction. In the absence of the second substrate methylenetetrahydrofolate, dUMP enhances the reaction of molecular oxygen with the reduced enzyme	Thermotoga maritima	a

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Release 2023.1 (January 2023)