Sandbox Reserved 1475: Difference between revisions
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The main function of this enzyme is to Retinoic acid. RalDH2 requires (NAD+) as a cofactor.<ref name="Lamb AL, Newcomber ME" /> In the oxidoreductase reaction, NAD+ acts as an electron acceptor. The reaction of this enzyme is [(retinal) + (NAD+) + (H2O) ↔ (retinoic acid) + (NADH) + (H+) ]. Once the NAD+ is bound, hydrogen bonds form with non-polar residues and one basic Lysine residue. Chloride ions participate in hydrophobic interactions with Arginine residues.<ref name="Lamb AL, Newcomber ME" /> Theres interactions cause a structural change to occur in the RalDH2 enzyme which causes it to form a more favorable folded confirmation. In the enzyme a large binding cavity is formed. | The main function of this enzyme is to Retinoic acid. RalDH2 requires (NAD+) as a cofactor.<ref name="Lamb AL, Newcomber ME" /> In the oxidoreductase reaction, NAD+ acts as an electron acceptor. The reaction of this enzyme is [(retinal) + (NAD+) + (H2O) ↔ (retinoic acid) + (NADH) + (H+) ]. Once the NAD+ is bound, hydrogen bonds form with non-polar residues and one basic Lysine residue. Chloride ions participate in hydrophobic interactions with Arginine residues.<ref name="Lamb AL, Newcomber ME" /> Theres interactions cause a structural change to occur in the RalDH2 enzyme which causes it to form a more favorable folded confirmation. In the enzyme a large binding cavity is formed. | ||
tructural changes occur to stabilize the tertiary structure of RalDH2 | tructural changes occur to stabilize the tertiary structure of RalDH2 | ||
== Structural highlights == | == Structural highlights == | ||
<Structure load='1bi9' size='350' frame='true' align='left' caption='[[Figure 2]] Nucleotide-Binding domain - orange, Catalytic domain - green, Tetramerization domain - blue (PDB entry [[1bi9]])' scene='80/800654/3_domains/3' /> | |||
The structure was based on the mitochondrial aldehyde dehydrogenase type two. RalDH2 in a monomer made up of 3 domains: a nucleotide-binding domain (1-136, 161-270), a catalytic domain (271-484), and a tetramerization domain (137-160, 485-484) as shown in [[Figure 1]].<ref name="Lamb AL, Newcomber ME" /> [[Image:3 Domains of RalDH2.png|thumb|upright=2| [[Figure 1]] Nucleotide-binding domain - orange, Catalytic domain - green, Tetramerization domain - blue. Imagine modified in Chimera from (PDB entry [[1bi9]]). Chain D shown with NAD substrate shown in pink]] | The structure was based on the mitochondrial aldehyde dehydrogenase type two. RalDH2 in a monomer made up of 3 domains: a nucleotide-binding domain (1-136, 161-270), a catalytic domain (271-484), and a tetramerization domain (137-160, 485-484) as shown in [[Figure 1]].<ref name="Lamb AL, Newcomber ME" /> [[Image:3 Domains of RalDH2.png|thumb|upright=2| [[Figure 1]] Nucleotide-binding domain - orange, Catalytic domain - green, Tetramerization domain - blue. Imagine modified in Chimera from (PDB entry [[1bi9]]). Chain D shown with NAD substrate shown in pink]] | ||
The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" ([[Figure 2]]). | The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" ([[Figure 2]]). | ||
</StructureSection> | |||
===Substrate NAD=== | ===Substrate NAD=== | ||
The crystal structure was cocrystallized with <scene name='80/800654/Nad/1'>NAD</scene>, and was determined at a 2.7 Angstrom resolution. <ref name="Lamb AL, Newcomber ME" /> | |||
== Disease == | |||
== Relevance == | |||
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</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
