Sandbox Reserved 1475: Difference between revisions
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With the cofactor NAD+ present the catalytic domain of RalDH2 is highly mobile and needs the selective substrate present to immobilize the catalytic domain. The binding of hydrophobic substrate and the NAD+ cofactor are needed to stabilize the catalytic domain.<ref name="Lamb AL, Newcomber ME" /> Short chain aldehydes do not have a large enough hydrophobic surface to bury inside the channel and therefor cannot work as suitable substrates. The long tails of the long chained aldehydes are needed to interact with the catalytic Cys-302 through hydrogen bonds. Short chained aldehydes can have hydrogen bond interactions with Cys-302 however are not large enough to fully bury the whole access channel, which is needed for the catalytic domain to be immobilized. | With the cofactor NAD+ present the catalytic domain of RalDH2 is highly mobile and needs the selective substrate present to immobilize the catalytic domain. The binding of hydrophobic substrate and the NAD+ cofactor are needed to stabilize the catalytic domain.<ref name="Lamb AL, Newcomber ME" /> Short chain aldehydes do not have a large enough hydrophobic surface to bury inside the channel and therefor cannot work as suitable substrates. The long tails of the long chained aldehydes are needed to interact with the catalytic Cys-302 through hydrogen bonds. Short chained aldehydes can have hydrogen bond interactions with Cys-302 however are not large enough to fully bury the whole access channel, which is needed for the catalytic domain to be immobilized. | ||
As seen in [[Figure 5]] <ref name="Cloning of cDNA Encoding an Aldehyde Dehydrogenase">DOI:10.1074/jbc.271.27.16288 /ref> | As seen in [[Figure 5]] <ref name="Cloning of cDNA Encoding an Aldehyde Dehydrogenase">DOI:10.1074/jbc.271.27.16288 /ref> | ||
== Disease == | == Disease == | ||
