Amino acid sequence in the region of the reactive serine residue of eel acetylcholinesterase

Schaffer, Norwood K.; Michel, Harry O.; Bridges, Alec F.

doi:10.1021/bi00739a027

Cited by 31 publications

(7 citation statements)

References 25 publications

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“…purified electric eel AChE was measured by Schaffer et al (1973) at pH 7.4, 25°C, using 0.0037 MACh. The activity of AChE and BChE in 1.0 mL of several body fluids is given in Table 6.…”

Section: Source: a Tack Et A! ( 1987)mentioning

confidence: 99%

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

Nigg

Knaak

2000

Reviews of Environmental Contamination and Toxicology

100

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“…purified electric eel AChE was measured by Schaffer et al (1973) at pH 7.4, 25°C, using 0.0037 MACh. The activity of AChE and BChE in 1.0 mL of several body fluids is given in Table 6.…”

Section: Source: a Tack Et A! ( 1987)mentioning

confidence: 99%

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

Nigg

Knaak

2000

Reviews of Environmental Contamination and Toxicology

100

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“…1). Equivalent-weight determinations and peptide analysis indicate that phosphorylation occurs only at a single serine residue, and the amino-acid sequence about this residue shows significant homology among the enzymes in this class (1,2). Three-dimensional structures of several serine hydrolases have been determined by x-ray crystallography, and further striking structural similarities have thus been revealed (3).…”

mentioning

confidence: 99%

Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.

Rosenberry¹

1975

Proc. Natl. Acad. Sci. U.S.A.

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Inferences about the catalytic mechanism of acetylcholinesterase (acetyicholine hydrolase, EC 3.1.1.7) are frequently made on the basis of a presumed analogy with chymotrypsin, EC 3.4.21.1. Although both enzymes are serine hydrolases, several differences in the steady-state kinetic properties of the two have been observed. In this report particujar attention is focused on the second-order reaction constant, kcat/KapD While the reported pH dependence and deuterium oxide isotope effect associated with this parameter for chymotrypsin are generally consistent with simple models involving rate-limiting general acid-base catalysis, this study finds a more complicated situation with acetylcholi- In the absence of the three-dimensional structure for acetylcholinesterase, inferences about its mechanism have been based both on studies of its substrate catalysis and on analogies drawn from chymotrypsin (see refs. 1, 12, and 13). Yet aside from the similarities which classify it as a serine hydrolase, acetylcholinesterase differs significantly from chymotrypsin both in size and in catalytic properties. 11S acetylcholinesterase is a tetramer of essentially identical catalytic subunits, each with a molecular weight of about 75,000 (14).' The active site includes an anionic group which aids in the binding of cationic substrates (see refs. 1, 12, and 13

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“…The rate of hydrolysis (specific activity, 100-130 mmol of ACh hydrolyzed hr-1 mg-1 of protein) of ACh by purified electric eel AChE was measured by Schaffer et al (1973) at pH 7.4, 25°C, using 0.0037 MACh. The activity of AChE and BChE in 1.0 mL of several body fluids is given in Table 6.…”

Section: Distribution Concentration and Specific Activitymentioning

confidence: 99%

Reviews of Environmental Contamination and Toxicology

2000

Reviews of Environmental Contamination and Toxicology

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Amino acid sequence in the region of the reactive serine residue of eel acetylcholinesterase

Cited by 31 publications

References 25 publications

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.

Reviews of Environmental Contamination and Toxicology

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