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==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, a functional convergance has inferred between amidase signature enzymes (such as FAAH) and other classes of serine proteases <ref name="3LJ6"/>.
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, a functional convergance has inferred between amidase signature enzymes (such as FAAH) and other classes of [http://en.wikipedia.org/wiki/Serine_protease serine proteases] <ref name="3LJ6"/>.


[[Image:3LJ6_Image4.png|400 px|left|thumb|Figure3: FAAH catalytic site with water molecules bound; Protein in green, Water molecules as red spheres, Measurements in orange]]
[[Image:3LJ6_Image4.png|400 px|left|thumb|Figure3: FAAH catalytic site with water molecules bound; Protein in green, Water molecules as red spheres, Measurements in orange]]

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OCA, R. Jeremy Johnson, Rachel Erkilla, Melissa Jones