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Comparative Study
. 1992 Apr 30;184(2):719-26.
doi: 10.1016/0006-291x(92)90649-6.

Mechanism of inhibition of cholinesterases by huperzine A

Y Ashani  1 , J O Peggins 3rd, B P Doctor
Affiliations
Comparative Study

Mechanism of inhibition of cholinesterases by huperzine A

Y Ashani et al. Biochem Biophys Res Commun. .

Abstract

Huperzine A, an alkaloid isolated from Huperzia serrata was found to reversibly inhibit acetylcholinesterases (EC 3.1.1.7) and butyrylcholinesterases (EC 3.1.1.8) with on- and off-rates that depend on both the type and the source of enzyme. Long-term incubation of high concentrations of purified cholinesterases (1-8 microM) with huperzine A did not show any chemical modification of huperzine A. A low dissociation constant KI was obtained for mammalian acetylcholinesterase-huperzine (20-40 nM) compared to mammalian butyrylcholinesterase-huperzine (20-40 microM). This indicates that the thermodynamic stability of huperzine-cholinesterase complex may depend on the number and type of aromatic amino acid residues in the catalytic pocket region of the cholinesterase molecule.

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