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Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products*
- Y. Nicolet, O. Lockridge, P. Masson, J. Fontecilla-Camps, F. Nachon
- Biology, ChemistryJournal of Biological Chemistry
- 17 October 2003
The crystal structures of several recombinant truncated human BChE complexes and conjugates are reported and a description for mechanistically relevant non-productive substrate and product binding is provided and is similar to a previously published theoretical model of this enzyme.
Comparison of butyrylcholinesterase and acetylcholinesterase.
Comparison of the structure and base composition of the genes may give clues to understanding the origin and evolution of AChE and BChE.
Abundant Tissue Butyrylcholinesterase and Its Possible Function in the Acetylcholinesterase Knockout Mouse
The generally high levels of BChE activity in tissues, including the motor endplate, and the observation that mice live without AChE, suggest that B ChE has an essential function in nullizygous mice and probably in wild‐type mice as well.
Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma.
Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine
Review of human butyrylcholinesterase structure, function, genetic variants, history of use in the clinic, and potential therapeutic uses.
- O. Lockridge
- BiologyPharmacology and Therapeutics
- 1 April 2015
DNA mutation associated with the human butyrylcholinesterase K-variant and its linkage to the atypical variant mutation and other polymorphic sites.
The K-variant phenotype was found to be associated with a DNA transition from guanine to adenine at nucleotide 1615, which caused an amino acid change from alanine 539 to threonine (GCA----ACA; Ala539----Thr); there was a 30% reduction of serum butyrylcholinesterase activity associated with this mutation.
Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase.
- A. Saxena, A. Redman, X. Jiang, O. Lockridge, B. P. Doctor
- Biology, ChemistryBiochemistry
- 2 December 1997
Volume calculations for the active site gorge showed that the poor inhibitory activity of ethopropazine toward acetylcholinesterase was due to the smaller dimension of the active sites gorge which was unable to accommodate the bulky inhibitor molecule.
Complete amino acid sequence of human serum cholinesterase.
An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase is 4-fold more efficient.
- W. Xie, C. Altamirano, C. Bartels, R. J. Speirs, J. Cashman, O. Lockridge
- BiologyMolecular pharmacology
It was concluded that a step leading to formation of the acyl-enzyme intermediate was rate-limiting, and persons with the atypical variant of BChE may experience severe or fatal cocaine intoxication when administered a dose of cocaine that is not harmful to others.