Butyrylcholinesterase

spinqualitylabelsall models Glycosylated human butyrylcholinesterase complex with choline, glycerol, sulfate and Cl- ions (PDB code 1p0m) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Butyrylcholinesterase (BChE) is an enzyme widely distributed throughout the body in humans, but particularly prevalent in serum, where it occurs as a tetramer of catalytic subunits. It is distinguished from the homologous enzyme, acetylcholinesterase, by its ability to hydrolyze the non-natural substrate butyrylcholine as well as the neurotransmitter, acetylcholine. Relevance BChE finds medical use as a bioscavenger for overcoming organophosphate (OP) nerve agent and insecticide intoxication by interacting rapidly with the toxic agents. Disease BChE biological role remains obscure, but mutations in the human BCHE gene result in prolonged post-surgical apnea due to the inability of the mutant BChEs to hydrolyse the local anaesthetic, succinylcholine. Structural highlights Like in the AChE structure, BChE active site is located at the bottom of a ca. 20A deep gorge. The active site of BChE is similar to that of AChE. Water molecule is shown as red sphere. The differences are noticed in the lining of the gorge were some of the aromatic residues in AChE are substituted by hydrophobic ones and in the active site acyl-binding pocket where 2 Phe residues are replaced by Leu and Val in BChE. 3D structures of BChE Butyrylcholinesterase 3D structures

Additional Resources

For additional information, see: Butyrylcholinesterase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Alexander Berchansky, Lakshmi Venkatachalam, David Canner, Jaime Prilusky, Michal Harel