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. Author manuscript; available in PMC: 2007 Jan 29.

Published in final edited form as: Bioorg Chem. 2006 Oct 27;34(6):362–379. doi: 10.1016/j.bioorg.2006.09.001

Inhibition of E1h by AcPhi () and AcMPhi (). E1h (0.649 μM) was incubated in 50 mM potassium phosphate buffer (pH 7.0), 2 mM MgCl₂, 0.2 mM ThDP with different concentrations of AcPhi or AcMPhi for 30 min. Aliquots were taken to determine activity of E1h in the PDHc assay as described in Materials and Methods. 100% of activity was determined in the absence of inhibitors in the incubation mixture and corresponds to 32 U/mg of E1h protein. Data points are means ± SE (n = 3-4). Inset shows inhibition of E1h by AcPhi at lower concentrations.

Inline graphic — Inhibition of E1h by AcPhi () and AcMPhi (). E1h (0.649 μM) was incubated in 50 mM potassium phosphate buffer (pH 7.0), 2 mM MgCl₂, 0.2 mM ThDP with different concentrations of AcPhi or AcMPhi for 30 min. Aliquots were taken to determine activity of E1h in the PDHc assay as described in Materials and Methods. 100% of activity was determined in the absence of inhibitors in the incubation mixture and corresponds to 32 U/mg of E1h protein. Data points are means ± SE (n = 3-4). Inset shows inhibition of E1h by AcPhi at lower concentrations.