<p>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.<br><br>Herein we include underpinning liquid chromatography - mass spectrometry data for this publication, acquired using EPSRC-funded equipment.<br><br>Researc results based upon these data are published at http://doi.org/10.1021/acs.biochem.6b01268<br></p><p><br></p>
Funding
Reaction-coupled dynamics in DHFR catalysis
Biotechnology and Biological Sciences Research Council