Sandbox Reserved 921: Difference between revisions

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== References ==
== References ==
<references/>
<ref>PMID:23581831</ref>


== Headline text ==
== Headline text ==

Revision as of 06:40, 4 April 2014

This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922.
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Fatty Acid Amide Hydrolase

Figure Legend


IntroductionIntroduction

Fatty acid amid hydrolase (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. FAAH is most commonly known for the degradation of anandamid[1], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid[2]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH.


FAAH

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FunctionFunction

ReferencesReferences


[1]

Headline textHeadline text

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, R. Jeremy Johnson, Carter Sharp, Daniel B. Lange