Mechanism of inhibition of cholinesterases by Huperzine A. (Reannouncement with new availability information)
Technical Report
·
OSTI ID:177463
Huperzine A, an alkaloid isolated from Huperzia serrata was found to reversibly inhibit acetylcholinesterases (EC 3.1.7) and (EC 3.1.1.8) with i 3.1 on- and off-rates that depend on both the type and the source of enzyme. Long incubation of high concentrations of purified (1-8 PM) with huperzine-A did not show any chemical modification of huperzine-A. A low dissociation constant K sub 1 was obtained for mammalian acetylcholinesterase-huperzine (20-40 nM) compared to mammalian butyrylcholinesterase-huperzine (20-40 microns.) 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.
- Research Organization:
- Walter Reed Army Inst. of Research, Washington, DC (United States)
- OSTI ID:
- 177463
- Report Number(s):
- AD-A--254440/1/XAB
- Country of Publication:
- United States
- Language:
- English
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