Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations.
作者： L F Neville , A Gnatt , R Padan , S Seidman , H Soreq
DOI: 10.1016/S0021-9258(17)45277-X
关键词: Xenopus 、 Mutant 、 Butyrylthiocholine 、 Biochemistry 、 Cholinesterase 、 Mutation 、 Amino acid 、 Butyrylcholinesterase 、 Biology 、 Dibucaine
摘要: Structure-function relationships of recombinant human butyrylcholinesterase (CHE) variants were investigated by Xenopus oocyte microinjection. A Ser-425 to Pro-425 mutation failed modify ligand binding properties. In contrast, Asp-70 Gly-70 substitution significantly reduced CHE capacity for succinylcholine and specific inhibitors, demonstrating as a key anionic site component certain ligands. Furthermore, the presence both mutations rendered totally resistant dibucaine inhibition, while all mutant proteins bound butyrylthiocholine, benzoylcholine, propionylcholine normally. These findings imply structural interactions between conserved regions in cholinesterases suggest contribution additional electronegative amino acids binding.
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