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 hydrophobic interaction | |||
White color indicates a polar interaction | |||
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 == | ||
<scene name='87/873227/Secondary_structure/1'>Secondary structure</scene> has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. | <scene name='87/873227/Secondary_structure/1'>Secondary structure</scene> has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. | ||
