Acetylcholine is a neurotransmitter found at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system. Entry of reference human-ACHE, (bromide 66-23-9 or chloride 60-31-1 or iodide 2260-50-6). So far the enzymes hydrolyzing acetylcholine in plants or bacteria are unrelated to animal AChE or any other alpha/beta hydrolases. The enzyme described by Rochu et al. in Pseudomonas fluorescens belongs to SBP_bac_8 (PF13416), the enzyme described by Sanchez et al. is a SGNH_hydrolase (CL0264). So called acetylcholinesterase of plants are also SGNH_hydrolase Yamamoto et al., Sagane et al.
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Title: Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Lockridge O Ref: Pharmacol Ther, 47:35, 1990 : PubMed
People with genetic variants of cholinesterase respond abnormally to succinylcholine, experiencing substantial prolongation of muscle paralysis with apnea rather than the usual 2-6 min. The structure of usual cholinesterase has been determined including the complete amino acid and nucleotide sequence. This has allowed identification of altered amino acids and nucleotides. The variant most frequently found in patients who respond abnormally to succinylcholine is atypical cholinesterase, which occurs in homozygous form in 1 out of 3500 Caucasians. Atypical cholinesterase has a single substitution at nucleotide 209 which changes aspartic acid 70 to glycine. This suggests that Asp 70 is part of the anionic site, and that the absence of this negatively charged amino acid explains the reduced affinity of atypical cholinesterase for positively charged substrates and inhibitors. The clinical consequence of reduced affinity for succinylcholine is that none of the succinylcholine is hydrolyzed in blood and a large overdose reaches the nerve-muscle junction where it causes prolonged muscle paralysis. Silent cholinesterase has a frame shift mutation at glycine 117 which prematurely terminates protein synthesis and yields no active enzyme. The K variant, named in honor of W. Kalow, has threonine in place of alanine 539. The K variant is associated with 33% lower activity. All variants arise from a single locus as there is only one gene for human cholinesterase (EC 3.1.1.8). Comparison of amino acid sequences of esterases and proteases shows that cholinesterase belongs to a new family of serine esterases which is different from the serine proteases.
Title: Hydrolysis by acetylcholinesterase. Apparent molal volumes and trimethyl and methyl subsites Hasan FB, Cohen SG, Cohen JB Ref: Journal of Biological Chemistry, 255:3898, 1980 : PubMed
Title: The action of normal and atypical cholinesterase of human serum upon a series of esters of choline Davies RO, Marton AV, Kalow W Ref: Canadian Journal of Biochemistry & Pharmacology, 38:545, 1960 : PubMed
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