Data underpinning "Reduction of Folate by Dihydrofolate Reductase from Thermotoga maritima"

We have shown that DHFR from the hyperthermophilic bacterium Thermotoga maritima is able to catalyse reduction of folate to tetrahydrofolate with a similar efficiency to reduction of dihydrofolate under saturating conditions. NMR and mass spectrometry experiments showed no evidence for production of free dihydrofolate during either the EcDHFR- or TmDHFR-catalysed reductions of folate, suggesting that both enzymes perform the two reduction steps without release of the partially reduced substrate. Herein we include underpinning liquid chromatography - mass spectrometry data.