Encyclopedia of toxicology. Wexler-P; Gad-SC, eds., San Diego, CA: Academic Press, 1998 1:326-340
Cholinesterases (ChEs) are a ubiquitous groups of enzymes that hydrolyze esters of choline. A well known example is acetylcholinesterase (AChE, acetyl choline hydrolase, EC 188.8.131.52), the enzyme responsible for hydrolyzing the important neurotransmitter acetylcholine (ACh). Another ChE is butyrylcholinesterase (BuChE, acylcholine acylhydrolase, EC 184.108.40.206), also known as nonspecific cholinesterase. The preferred substrate for AChEs is ACh; BuChEs prefer to hydrolyze esters like butyrylcholine and propionylcholine. Both AChE and BuChE are inhibited by some organophosphate (OP) and carbamate (CB) esters, and also by other chemicals. Many ChE inhibitors act at the catalytic site of the enzyme, forming enzyme-inhibitor complexes that are slow to hydrolyze. The use of ChE inhibitors as insecticides and as chemical warfare agents, their toxicity to humans, and their impact on wildlife have made them important to toxicology researchers and, public health and environmental health officials.
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