Article
Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase.
Biochimica et biophysica acta - 12 Jan 2001
Masson P, Xie W, Froment M T, Lockridge O
Abstract excerpt
The peripheral anionic site (PAS) of human butyrylcholinesterase is involved in the mechanism of substrate activation by positively charged substrates and ligands. Two substrate binding loci, D70 in the PAS and W82 in the active site, are connected by the Omega loop. To determine whether the Omega loop plays a role in the signal transduction between the PAS and the active site, residues involved in stabilization...
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