Sandbox Reserved 1665: Difference between revisions
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:Trp 160, Tyr 163, Trp 450, Phe 456, Tyr 458, Met 114, Leu 118 | :Trp 160, Tyr 163, Trp 450, Phe 456, Tyr 458, Met 114, Leu 118 | ||
There are a couple of <scene name='87/873227/Intermolecular_forces/3'>intermolecular forces</scene> involved in the protein like <scene name='87/873227/Hydrophobic_interaction/2'>hydrophobic bonds</scene>, hydrogen bonds, polar interactions, <scene name='87/873227/Negatively_charged_acidic_bond/2'>negatively charged/acidic interactions</scene>, and positively charged/ basic interactions. | There are a couple of <scene name='87/873227/Intermolecular_forces/3'>intermolecular forces</scene> involved in the protein like <scene name='87/873227/Hydrophobic_interaction/2'>hydrophobic bonds</scene>, hydrogen bonds, polar interactions, <scene name='87/873227/Negatively_charged_acidic_bond/2'>negatively charged/acidic interactions</scene>, and <scene name='87/873227/Positively_charged_basic/1'>positively charged/ basic</scene> interactions. | ||
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. | ||
