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Acetylcholinesterase from Electrophorus electricus (electric eel)

BioChemika, powder, slightly yellow, ~850 units/mg, from Electrophorus electricus

Synonym

Acetylcholine acetylhydrolase

AChE

Cholinesterase, Acetyl

CAS Number

9000-81-1

Enzyme Commission (EC) Number

3.1.1.7 ( BRENDA | IUBMB )

MDL number

MFCD00081268

EG/EC Number

232-559-3

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Descriptions

Biochem/physiol Actions

Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H₂O to choline + acetic acid.

Other Notes

Association with sphingomyelin liposomes. Relevance to collagen-sphingomyelin interactions¹; Enzyme immunoassay of eicosanoids²; Application in (selective) hydrolysis/condensation of carboxylic ester bonds^3,⁴

Unit Definition

One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C.

General description

Molecular Weight: 280 kDa
Isoelectric Point: 5.5
Extinction Coefficient: E^1% = 18.0 (280 nm)

Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.

Properties

biological source

from Electrophorus electricus

product line

BioChemika

form

powder

mol wt

M_r ~250000

color

slightly yellow

shipped in

dry ice

storage temp.

−20°C

References

Cited Reference

1. R. Cohen, Y. Barenholz Biochim. Biophys. Acta 778, 94, (1984) abstract

2. P. Pradelles et al. Meth. Enzymol. 187, 24, (1990) abstract

3. D.R. Deardorff et al. Tet. Lett. 27, 1255, (1986)

4. C.R. Johnson, Th.D. Penning J. Am. Chem. Soc. 110, 4726, (1988)

Reference

Levinson, S., and Ellory, J., The molecular form of acetylcholinesterase as determined by irradiation inactivation. Biochem. J. 137, 123-125, (1974)

Anglister, I., and Silman, I., Molecular structure of elongated forms of electric eel acetylcholinesterase. J. Mol. Biol. 125, 293-311, (1978)

Froede, H.C., and Wilson I.B., Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J. Biol. Chem. 259, 11010-11013, (1984)

Szegletes, T., et al., Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38, 122-133, (1999)

Taylor, P., The cholinesterases. J. Biol. Chem. 266, 4025-4028, (1991)

Rosenberry, T.L., et al., Structure of the 11S acetylcholinesterase. Subunit composition. Biochemistry 13, 3068-3079, (1974)

Safety

WGK Germany

10-21

Related Categories

... General Metabolic Enzymes > General Metabolic Enzymes A-H

... Enzyme-Mediated Synthesis > Hydrolases

... 3.x.x.x Hydrolases > 3.1.x.x Acting on esters

MSDS

Certificate of Analysis

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