Sandbox Reserved 911: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 16: | Line 16: | ||
==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. (IMT5) | 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. (IMT5) | ||
FAAH requires two water molecules in its active site to properly cleave amide bonds. One water molecule (W1) deacylates the substrate, and the other (W2) helps coordinate W1 through the catalytic K142. (3LJ6) | FAAH requires two water molecules in its active site to properly cleave amide bonds. One water molecule (W1) deacylates the substrate, and the other (W2) helps coordinate W1 through the catalytic K142. (3LJ6) | ||
[[Image:Water_image.png|400 px|left|thumb|FAAH catalytic site with water molecules bound]] | [[Image:Water_image.png|400 px|left|thumb|FAAH catalytic site with water molecules bound]] | ||
==Heading 4== | |||
</StructureSection> | </StructureSection> | ||
