Characterization of a non-nudix pyrophosphatase points to interplay between flavin and NAD(H) homeostasis in Saccharomyces cerevisiae
Fig 1
Analysis of substrate binding of Fpy1p.
(A) Substrate specificity of Fpy1p. Data are expressed as a percent of activity relative to that observed when FAD is used as substrate with each metal ion, and is given as the average ± S.E. of three triplicate determinations in which AMP production was quantified. Assays were performed with 100 μM substrate along with either 4 mM CoCl2 (cobalt) or 10 mM MgCl2 (magnesium). (B) FAD pyrophosphatase activity of Fpy1p in the presence of potential inhibitors. Data are shown as the average ± S.E. of three triplicate determinations in which FMN production was quantified. Assays were performed using 4 mM CoCl2, 20 μM FAD, and 50 μM lumiflavin or nicotinamide when specified. Higher concentrations were not used due to limited solubility of lumiflavin.