Sandbox Reserved 911: Difference between revisions
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==Hydrolase Information== | ==Hydrolase Information== | ||
Crystal structures of FAAH show that the enzyme is a homodimer in solution, with each subunit having a mass of 63 kD. The protein's <scene name='57/573125/2vya/8'>twisted Beta sheet core</scene> of 11 strands is surrounded by 24 alpha helices. The enzyme is embedded in the cell membrane to catch the lipid signaling molecules that can diffuse through membranes. The FAAH structure shows an entry channel leading from the lipid bilayer to the enzyme's active site, providing a path for endocannabinoids to enter the hydrolase. In addition, FAAH possesses a channel leading from the active site to the cell's cytoplasm, allowing the release of polar compounds released from lipid cleavage and the entry of water molecules necessary for the FAAH mechanism to proceed. | Crystal structures of FAAH show that the enzyme is a homodimer in solution, with each subunit having a mass of 63 kD. The protein's <scene name='57/573125/2vya/8'>twisted Beta sheet core</scene> of 11 strands is surrounded by 24 alpha helices. The enzyme is embedded in the cell membrane to catch the lipid signaling molecules that can diffuse through membranes. The FAAH structure shows an entry channel leading from the lipid bilayer to the enzyme's active site, providing a path for endocannabinoids to enter the hydrolase. In addition, FAAH possesses a channel leading from the active site to the cell's cytoplasm, allowing the release of polar compounds released from lipid cleavage and the entry of water molecules necessary for the FAAH mechanism to proceed. | ||
<scene name='57/573125/2vya/1'>humanized rat FAAH dimer</scene> with <scene name='57/573125/2vya/3'>PF-750 inhibitor</scene> | <scene name='57/573125/2vya/1'>humanized rat FAAH dimer</scene> with <scene name='57/573125/2vya/3'>PF-750 inhibitor</scene> | ||
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===Catalytic Triad=== | ===Catalytic Triad=== | ||
Mutagenesis and inhibitor studies have shown that FAAH has a <scene name='57/573125/2vya/6'>Ser-Ser-Lys catalytic triad</scene>, consisting of S241, S217, and K142. Ser-Ser-Lys catalytic triads are not often seen in hydrolases, making FAAH an enzyme of interest for additional research. S241 acts as the catalytic nucleophile for the cleavage of amide bonds. | Mutagenesis and inhibitor studies have shown that FAAH has a <scene name='57/573125/2vya/6'>Ser-Ser-Lys catalytic triad</scene>, consisting of S241, S217, and K142. Ser-Ser-Lys catalytic triads are not often seen in hydrolases, making FAAH an enzyme of interest for additional research. S241 acts as the catalytic nucleophile for the cleavage of amide bonds. | ||
[[Image:Water_image.png|400 px|left|thumb|FAAH catalytic site with water molecules bound]] | |||
</StructureSection> | </StructureSection> | ||
