Sandbox Reserved 1665: Difference between revisions

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In the article, there were other substrates mentioned that were detected in AldC by using spectrophotometric assay. Substrates that were identified were aliphatic aldehydes of 5–9-carbon length, like hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde. As substrates, octanal had the highest specific activity that function properly for AldC. The article also mentions that short 2–4-carbon aldehydes, branched aliphatic aldehydes, and larger aromatic aldehydes are poor substrates for AldC.
In the article, there were other substrates mentioned that were detected in AldC by using spectrophotometric assay. Substrates that were identified were aliphatic aldehydes of 5–9-carbon length, like hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde. As substrates, octanal had the highest specific activity that function properly for AldC. The article also mentions that short 2–4-carbon aldehydes, branched aliphatic aldehydes, and larger aromatic aldehydes are poor substrates for AldC.


https://proteopedia.org/wiki/images/3/3a/AldC_activie_sites.PNG


(In the figure above it shows the active sites for AldC)
Red color indicated a <scene name='87/873227/Hydrophobic_interaction/1'>hydrophobic interaction</scene>
White color indicates a <scene name='87/873227/Polar_interaction/1'>polar interaction</scene>
Side chains interacting with Octanal are green
Side chains interacting with NAD are blue.
There are two water molecules (red spheres) interacting with the cofactor NAD
Hydrogen bonds interactions between amino acid residues and ligands are in yellow


== Structural highlights ==
== Structural highlights ==
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