User:Kaitlyn Enderle/Sandbox 1

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== Dimethylarginine Dimethylaminohydrolase I ''Bos Taurus'' ==
== Dimethylarginine Dimethylaminohydrolase I ''Bos Taurus'' ==
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<StructureSection load='2cI3' size='340' side='right' caption='Dimethylarginine Dimethylaminohydrolase' scene='75/752351/Ddah_loop/2'>
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<StructureSection load='2cI3' size='340' side='right' caption='Dimethylarginine Dimethylaminohydrolase' scene='75/752351/Ddah/1'>DDAH</scene>
This is a default text for your page '''Kaitlyn Enderle/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Kaitlyn Enderle/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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<scene name='75/752351/Ddah_loop/2'>lid region</scene>
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<scene name='75/752351/Ddah/2'>Dimethylarginine Dimethylaminohydrolase</scene>
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== Function ==
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<scene name='75/752351/Ddah_water_pore/12'>channel</scene>
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== Disease ==
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<scene name='75/752351/Ddah_salt_bridge/5'>salt bridge</scene>
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== Relevance ==
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<scene name='75/752351/Ddah_active_site/3'>active site</scene>
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DDAH works to hydrolyze MMA and ADMA. Both MMA and ADMA competitively inhibit NO synthesis by inhibiting Nitric Oxide Synthase (NOS). Because NO is highly toxic, freely diffusible across membranes, and its radical form is fairly reactive, cells must maintain a large control on concentrations by regulating NOS activity and the activity of enzymes such as DDAH that have an indirect effect of the concentration of NO. An imbalance of NO contributes to several diseases. Low NO levels, potentially caused by low DDAH activity and therefore high MMA and ADMA concentrations, have been implicated with diseases such as uremia, chronic heart failure, atherosclerosis, and hyperhomocysteinemia. High levels of NO have been involved with diseases such as septic shock, migraine, inflammation, and neurodegenerative disorders. Because of the effects on NO levels and known inhibitors to DDAH, regulation of DDAH may be an effective way to regulate NO levels therefore treating the diseases.
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== Structural highlights ==
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<scene name='75/752351/Ddah_water_pore/13'>water-filled pore</scene>
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==Inhibitors==
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<scene name='75/752351/Lid_focus/2'>loop region</scene>
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===Zinc at pH 6.3===
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===Zinc at pH 9===
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===L-Citrulline===
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===L-Homocystine===
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[[Image:P56965_with_homo.gif |300 px|left|thumb|Figure Legend ]]
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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<scene name='75/752351/Hbond_leu29/3'>hydrogen bond</scene>
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</StructureSection>
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<scene name='75/752351/Ddah_active_site/4'>Cys249</scene>
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== References ==
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<references/>
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<scene name='75/752351/Ddah_active_site_his162/2'>His162</scene>
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<scene name='75/752351/Ddah_salt_bridge/6'>salt bridge</scene>
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<scene name='75/752351/Ddah_water_pore/14'>delineated</scene>
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<scene name='75/752351/Ddah_water_pore/15'>His172 and Ser175</scene>
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<scene name='75/752351/Ddah_l-homocysteine/3'>L-homocysteine</scene>
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<scene name='75/752351/Ddah_with_l-citrulline/5'>L-citrulline</scene>
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<scene name='75/752351/Ddah_s-nitroso-l-homocysteine/4'>S-nitroso-L-homocysteine</scene>
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<scene name='75/752351/Hbond_leu29/4'>4 hydrogen bonds</scene>
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<scene name='75/752351/Hbond_leu29/6'>Hydrogen bonds</scene> -attacked by Cys249
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<scene name='75/752351/Hbond_leu29/7'>salt bridges</scene>

Current revision

Dimethylarginine Dimethylaminohydrolase I Bos Taurus

Dimethylarginine Dimethylaminohydrolase

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Proteopedia Page Contributors and Editors (what is this?)

Kaitlyn Enderle

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