Sandbox 177: Difference between revisions
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CYPOR is a ~78kDa, multidomain flavoprotein.<ref name="5TSON">PMID:19171935</ref> Containing three co-factors, <scene name='Sandbox_177/Cyporfmn/2'>FMN</scene>, <scene name='Sandbox_177/Cyporfad/2'>FAD</scene> and <scene name='Sandbox_177/Cypornadph/2'>NADPH</scene>, CYPOR is the archetype for the mammalian diflavin-containing enzyme family.<ref name="5TSON"/> Research indicates that the protein, and other FAD/FMN binding proteins, are likely the product of the fusion of two ancestral genes.<ref name="6TSON">PMID:8078947</ref> This would account for the two distinct binding domain areas, FMN and FAD/NADPH, which each provide different functional capabilities to the overall protein.<ref name="6TSON"/> | CYPOR is a ~78kDa, multidomain flavoprotein.<ref name="5TSON">PMID:19171935</ref> Containing three co-factors, <scene name='Sandbox_177/Cyporfmn/2'>FMN</scene>, <scene name='Sandbox_177/Cyporfad/2'>FAD</scene> and <scene name='Sandbox_177/Cypornadph/2'>NADPH</scene>, CYPOR is the archetype for the mammalian diflavin-containing enzyme family.<ref name="5TSON"/> Research indicates that the protein, and other FAD/FMN binding proteins, are likely the product of the fusion of two ancestral genes.<ref name="6TSON">PMID:8078947</ref> This would account for the two distinct binding domain areas, FMN and FAD/NADPH, which each provide different functional capabilities to the overall protein.<ref name="6TSON"/> | ||
Regulation of this protein, which is found all tissues to some extent, is largely at the transcriptional level.<ref name="3cTSON">PMID:11306680</ref> The thyroid hormone T3 in most cases, while adrenocorticotrophic hormone acts as a regulator in a few specific cases.<ref name="3aTSON">PMID:2495435</ref><ref name="3bTSON">PMID:1737785</ref> | Regulation of this protein, which is found all tissues to some extent, is largely at the transcriptional level.<ref name="3cTSON">PMID:11306680</ref> The thyroid hormone T3 acts as a hormonal regulator in most cases, while adrenocorticotrophic hormone acts as a regulator in a few specific cases.<ref name="3aTSON">PMID:2495435</ref><ref name="3bTSON">PMID:1737785</ref> | ||
==='''Structure'''=== | ==='''Structure'''=== | ||
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As part of the microsomal electron transport system, CYPOR moves electrons from: | As part of the microsomal electron transport system, CYPOR moves electrons from: | ||
'''<span style="background-color:#FFA07A">NADPH</span> → <span style="background-color:#F0E68C">FAD</span> → <span style="background-color:#98FB98">FMN</span> → <span style="background-color:#AFEEEE">Cytochrome P450</span>''' | :::'''<span style="background-color:#FFA07A">NADPH</span> → <span style="background-color:#F0E68C">FAD</span> → <span style="background-color:#98FB98">FMN</span> → <span style="background-color:#AFEEEE">Cytochrome P450</span>''' | ||
Specifically a hydride anion is moved from NADPH to the FAD. The two electrons are then individually passed to FMN, in a process that is believed to be conformationally gated, before being passed on to cytochrome P450, again one at a time.<ref name="5TSON"/> This reduction of cytochrome P450 allows it to function in biosynthesis and biodegradation pathways of a variety of endogenous and foreign hydrophobic substrates, including drugs and steroids.<ref name="5TSON"/><ref name="2TSON">PMID:7743131</ref> | Specifically a hydride anion is moved from NADPH to the FAD. The two electrons are then individually passed to FMN, in a process that is believed to be conformationally gated, before being passed on to cytochrome P450, again one at a time.<ref name="5TSON"/> This reduction of cytochrome P450 allows it to function in biosynthesis and biodegradation pathways of a variety of endogenous and foreign hydrophobic substrates, including drugs and steroids.<ref name="5TSON"/><ref name="2TSON">PMID:7743131</ref> | ||
