Fatty acid amide hydrolase: Difference between revisions
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<StructureSection load='2VYA' size='350' side='right' caption='Fatty Acid Amide Hydrolase 1 (PDB: [[2vya]])' scene=''> | <StructureSection load='2VYA' size='350' side='right' caption='Fatty Acid Amide Hydrolase 1 (PDB: [[2vya]])' scene=''> | ||
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==Introduction== | ==Introduction== | ||
Fatty acid amide hydrolase (FAAH) degrades fatty acid amides (FAAs) to terminate their signaling activity <ref name="1MT5">PMID:12459591</ref>. A serine hydrolase from the [http://en.wikipedia.org/wiki/Amidase Amidase] signature superfamily of enzymes ([http://proteopedia.org/wiki/index.php/Category:Amidase other amidases]), FAAH degrades endocannabinoid signaling lipids, molecules associated with pain relief <ref name="2WAP">PMID:19389627</ref>. Because [http://en.wikipedia.org/wiki/Endocannabinoid_system endocannabinoids] are lipid molecules, they cannot be compartmentalized in vesicles (the degradation method for other neurotransmitters) and must instead be degraded in the bilayer of the cell membrane. FAAH is an [http://stevens.scripps.edu/images/faah_fig2.jpg integral membrane protein] that degrades FAAs as they enter the membrane bilayer, allowing the cell to terminate the activity of signaling molecules that cannot be contained within a vesicle for degredation <ref name="1MT5"/>. Current FAAH research aims to find inhibitors for the enzyme, which would prolong the pain alleviation provided by endocannabinoid molecules <ref name="2WAP"/>. | Fatty acid amide hydrolase (FAAH) degrades fatty acid amides (FAAs) to terminate their signaling activity <ref name="1MT5">PMID:12459591</ref>. A serine hydrolase from the [http://en.wikipedia.org/wiki/Amidase Amidase] signature superfamily of enzymes ([http://proteopedia.org/wiki/index.php/Category:Amidase other amidases]), FAAH degrades endocannabinoid signaling lipids, molecules associated with pain relief <ref name="2WAP">PMID:19389627</ref>. Because [http://en.wikipedia.org/wiki/Endocannabinoid_system endocannabinoids] are lipid molecules, they cannot be compartmentalized in vesicles (the degradation method for other neurotransmitters) and must instead be degraded in the bilayer of the cell membrane. FAAH is an [http://stevens.scripps.edu/images/faah_fig2.jpg integral membrane protein] that degrades FAAs as they enter the membrane bilayer, allowing the cell to terminate the activity of signaling molecules that cannot be contained within a vesicle for degredation <ref name="1MT5"/>. Current FAAH research aims to find inhibitors for the enzyme, which would prolong the pain alleviation provided by endocannabinoid molecules <ref name="2WAP"/>. | ||
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[[6dhv]] – AtFAAH – ''Arabidopsis thaliana''<BR /> | [[6dhv]] – AtFAAH – ''Arabidopsis thaliana''<BR /> | ||
[[6dii]] –AtFAAH + methyl linolenyl fluorophosphonate<BR /> | [[6dii]] –AtFAAH + methyl linolenyl fluorophosphonate<BR /> | ||
[[6kvr]] – FAAH – ''Candida albicans''<BR /> | |||
</StructureSection> | </StructureSection> | ||