Role of ionic interactions in cholinesterase catalysis.
Acetylcholinesterase (AChE, EC 3.1.1.7) is an enzyme terminating the transmission of nerve impulse in synapses by rapid and selective hydrolysis of the neurotransmitter acetylcholine. Recent years have added a considerable amount of structural knowledge about this protein as well as opened new perspectives to the study of the molecular mechanism of cholinesterase catalysis. In this paper the current state of understanding the molecular recognition by cholinesterases is critically surveyed with particular emphasis on the role of electrostatic interactions.
Tõugu
V
V
Laboratory of Bioorganic chemistry, Institute of Chemical Physics and Biophysics of the Estonian Academy of Sciences, Tallinn, Estonia. tougu@kbfi.ee
Kesvatera
T
T
D000494:Allosteric Regulation / Q000502:physiology; D001665:Binding Sites; D002219:Carbamates / Q000494:pharmacology; D002802:Cholinesterases / Q000737:chemistry / Q000378:metabolism*; D004058:Diffusion; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D012492:Salts / Q000494:pharmacology; D013379:Substrate Specificity
D002219:Carbamates; D004791:Enzyme Inhibitors; D012492:Salts; D002802:Cholinesterases