Sandbox Reserved 1475
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== Function == | == Function == | ||
| - | 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 confirmation. | + | 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 | ||
== Disease == | == Disease == | ||
Revision as of 00:57, 5 December 2018
</StructureSection>
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Contents |
Retinal Dehydrogenase Type Two Structure
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This molecular structure is Retinal Dehydrogenase Type Two (RalDH2). This enzyme is part of the super family Aldehyde Dehydrogenase. The function of this enzyme is to catalyze the oxidation of retinal to retinoic acid. Retinoic acid produces a putative morphogen that initiates pattern formation in the early embryo.[1] This is the last step in the formation of the hormone from Vitamin A (retinol). RalDH2 is expressed in Escherichia coli strain BL21(DE3) [2]
Function
The main function of this enzyme is to Retinoic acid. RalDH2 requires (NAD+) as a cofactor.[1] 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.[1] 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
Disease
Relevance
Structural highlights
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</StructureSection>
References
- ↑ 1.0 1.1 1.2 Lamb AL, Newcomer ME. The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity. Biochemistry. 1999 May 11;38(19):6003-11. PMID:10320326 doi:10.1021/bi9900471
- ↑ Lamb AL, Wang X, Napoli JL, Newcomer ME. Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II. Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):639-42. PMID:9761861
