Sandbox Reserved 911: Difference between revisions
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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. (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 to better determine how proteins with this catalytic triad function. 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]] | ||
==Relationship to other proteins== | ==Relationship to other proteins== | ||
The hydrolytic water molecules important to FAAH's function suggest an evolutionary relationship of this hydrolase to other enzymes. The structures of other [http://en.wikipedia.org/wiki/Serine_hydrolase serine hydrolases] also display a catalytic water molecule in their active sites. Because hydrolases that are non-homologous to FAAH also require a water molecule to cleave bonds, | The hydrolytic water molecules important to FAAH's function suggest an evolutionary relationship of this hydrolase to other enzymes. The structures of other [http://en.wikipedia.org/wiki/Serine_hydrolase serine hydrolases] also display a catalytic water molecule in their active sites. Because hydrolases that are non-homologous to FAAH also require a water molecule to cleave bonds, researchers have inferred that a functional convergance has developed between amidase signature enzymes (such as FAAH) and other classes of serine proteases. (3LJ6) | ||
</StructureSection> | </StructureSection> | ||
