Sandbox Reserved 1677: Difference between revisions
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=== Function of your protein === | === Function of your protein === | ||
<scene name='87/873239/Image_of_ligand/1'>Aldehyde dehydrogenases</scene> serve as | <scene name='87/873239/Image_of_ligand/1'>Aldehyde dehydrogenases</scene> serve as metabolic housekeeping enzymes due to their ability to detoxify aldehydes, which are highly reactive compounds generated through cellular. They can also scavenge aldehyde from lipid peroxidation and convert them to a less chemically reactive carboxylic acid. Aldc additionally play an important role in ethanol metabolism via oxidation of acetaldehyde into acetate, metabolism of polyamine, and plant cell wall ester biogenesis. The bacterial pathogen Pseudomonas syringae is the organism that is causing mutation in the host. | ||
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. | 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. | ||
