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Literature summary for 2.1.1.45 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.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
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Reaction

Reaction Comment Organism Reaction ID
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