Sandbox Reserved 1677: Difference between revisions

In order to determine the substrate preference of AldC, a panel of 23 molecules including short to long chain aliphatic aldehydes was used to screen for enzymatic activity. Spectrophotometric assays of AldC identified aliphatic aldehydes of 5-9 carbon length as substrates. It turns out that the 8 carbon carbon substrate is the preferred aliphatic aldehyde substrate in this case Octanal, which is surrounded by aromatic rings. On the comparison table, data suggest that short 2-4 carbon aldehydes, branched aliphatic aldehydes and larger aromatic aldehydes are poor substrates.It turns out that 8 carbon carbon substrate is the preferred aliphatic aldehyde substrate in this case Octanal, which is surrounded by aromatic rings. To evaluate the nicotinamide cofactor preference for AldC, the activity of the enzyme was tested either with octanal and NADP+ or NAD+, which showed a distinct preference for NAD+. octanal has the highest Kcat value and lowest Km value which increases its efficiancy.