C3389
Sigma

Acetylcholinesterase from Electrophorus electricus (electric eel)

Type VI-S, lyophilized powder, 200-1,000 units/mg protein

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

Expand/Collapse All

Descriptions

Analysis Note

The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.

Biochem/physiol Actions

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

Unit Definition

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

Physical form

Lyophilized powder containing Tris buffer salts

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

type

Type VI-S

form

lyophilized powder

composition

Protein, ≥60% biuret

storage temp.

−20°C

References

Reference

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

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

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)

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

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

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)

Safety

WGK Germany

10-21