Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates.

doi:10.1016/s0167-4838(99)00115-6

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Article

Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates.

Biochimica et biophysica acta - 17 Aug 1999

Masson P, Xie W, Froment M T, Levitsky V, Fortier P L, Albaret C, Lockridge O

Abstract excerpt

Human butyrylcholinesterase displays substrate activation with positively charged butyrylthiocholine (BTC) as the substrate. Peripheral anionic site (PAS) residues D70 and Y332 appear to be involved in the initial binding of charged substrates and in activation control. To determine the contribution of PAS residues to binding and hydrolysis of quaternary substrates and activation control, the single mutants...

Topics

Binding Sites
Butyrylcholinesterase
Butyrylthiocholine
Cholinesterase Inhibitors
Humans
Kinetics
Mutation
Protein Conformation
Quaternary Ammonium Compounds
Substrate Specificity
Thermodynamics

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Open in PubMed

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PMID: 10446378
DOI: 10.1016/s0167-4838(99)00115-6

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