Acetylcholinesterase

Rosenberry, Terrone L.

doi:10.1002/9780470122884.ch3

Cited by 211 publications

(124 citation statements)

References 230 publications

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“…The reaction is very fast, approaching the diffusion limit. 1,2 However, one of the peculiarities of this single catalytic subunit of the enzyme revealed from the X-ray structure is that the active site (AS) resides in a deeply buried gorge, whose entrance is not even wide enough for the entrance of the substrate ACh. 3 So it is difficult for us to understand how such a rapid enzyme at its AS is buried close to the bottom of the deep and narrow gorge.…”

Section: Introductionmentioning

confidence: 99%

Research on the regulation of the spatial structure of acetylcholinesterase tetramer with high efficiency by AFM

Jiang¹,

Wang²,

Xi³

et al. 2013

IJN

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Atomic force microscopy (AFM) was applied for obtaining structural information about acetylcholinesterase (AChE) tetramer (AChE G 4 ) before and after reaction with S-acetylcholine iodide (S-ACh), in the presence or absence of propidium iodide (PI), an inhibitor for peripheral anionic sites (PAS). An iced-bath ultrasound was used to prepare the phospholipid membrane. Ves-fusion technique was applied for incorporating AChE G 4 in a lipid layer on mica. Before reaction with substrates, the single AChE G 4 particle was ellipsoid in shape with a clear border. It had a smooth surface with a central projection. The four subunits of a single enzyme particle were arranged tightly (no separated subunits being found, with an average size of 89 ± 7 nm in length, 68 ± 9 nm in width, and 6 ± 3 nm in height). After reaction with S-ACh in the absence of PI, the loose arrangement of subunits of AChE G 4 was seen, with an average size of 104 ± 7 nm in length, 91 ± 5 nm in width, and 8 ± 2 nm in height. Also there was free-flowing space amongst the four subunits of the AChE G 4 . This was consistent with the results of the Χ-ray diffraction crystallography and molecular dynamics studies. The apparent free space was the central path of AChE G 4 , changing from small to big, to small, to lateral door appearance, with an average size of 60 ± 5 nm in length and 51 ± 9 nm in width. The size of lateral door was 52 ± 5 nm in width and 32 ± 3 nm in depth on average. In the presence of PI, S-ACh could not cause topological structure changes of AChE G 4 . AFM verified that the central path might govern the turnover of the enzyme morphologically, and the interactions between PI and S-ACh might gate the creation of a central path and the opening of ACG in monomer; and the combination of S-ACh with peripheral anionic sites is conducive to the opening of ACG while PI can inhibit this action. Resolution at the inframolecular level is favorable in providing substantial information on how the spatial structure is adapted to the high efficiency of AChE molecules.

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Section: Introductionmentioning

confidence: 99%

Research on the regulation of the spatial structure of acetylcholinesterase tetramer with high efficiency by AFM

Jiang¹,

Wang²,

Xi³

et al. 2013

IJN

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“…1 AChE terminates a nervous transmission via degrading a neurotransmitter acetylcholine within the synaptic cleft. 2 Cavity of the enzyme is located in 20 Å (20 nm) deep gorge with active (A) site and peripheral (P) site. 3,4 A-site contains amino-acids residues of catalytic triad (S203, E334 and H447).…”

Section: Introductionmentioning

confidence: 99%

In vitro Screening of Oxime Reactivators on the Model of Paraoxon-inhibited Acetylcholinesterase-SAR Study

Holas¹,

Musílek²,

Pohanka³

et al. 2010

Bulletin of the Korean Chemical Society

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Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 µM and 10 µM). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.

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“…[1][2][3][4] In honeybees and other insects, most of the AChE activity is found in the central nervous system, rather than in the peripheral nervous system. 5 Many compounds including organophosphorus and carbamate insecticides are commonly used to quasi-irreversibly inhibit AChE.…”

Section: Introductionmentioning

confidence: 99%

Development of an Acetylcholinesterase-Based Detection Kit for the Determination of Organophosphorus and Carbamate Pesticide Residues in Agricultural Samples

Kim¹,

El‐Aty²,

Hwang³

et al. 2007

Bulletin of the Korean Chemical Society

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The objective of this study was to develop a rapid, simple, and qualitative acetylcholinesterase (AChE)-detection kit, based on a modification of the Ellman and ELISA methods, for the detection of organophosphorus (OP) and carbamate (CB) pesticide. The developed kits were used to screen a large number of agricultural samples (spiked and real) for OP and CB pesticide residues. AChE was extracted from the heads of honeybees (Apis mellifera L.) using Triton X-100, and was purified through 3 steps: diethylaminoethylcellulose chromatography (DEAE), affinity chromatography and membrane filtering, and Mono-Q column chromatography. Epoxy-activated Sepharose 6B affinity chromatography was used for large-scale purification. The presence of OP and CB pesticide residues in agricultural samples was assayed on the basis of AchE inhibition value. The presence (6 bands) or absence of some colored bands on the test line indicated a negative or positive result, respectively. The limits of detection for measured organophosphorus (OP) and carbamates (CB) pesticide residues in standard pesticide solutions and fortified samples were ranged from 0.50 to 2.50 ppm and 0.50 to 4.75 ppm, respectively.

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Acetylcholinesterase

Cited by 211 publications

References 230 publications

Research on the regulation of the spatial structure of acetylcholinesterase tetramer with high efficiency by AFM

Research on the regulation of the spatial structure of acetylcholinesterase tetramer with high efficiency by AFM

In vitro Screening of Oxime Reactivators on the Model of Paraoxon-inhibited Acetylcholinesterase-SAR Study

Development of an Acetylcholinesterase-Based Detection Kit for the Determination of Organophosphorus and Carbamate Pesticide Residues in Agricultural Samples

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