Acetylcholinesterase: Difference between revisions
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help attract and bind the basic, positively charged acetylcholine substrate, although are are some acidic residues nearby. Instead, bulky aromatic residues <scene name='Acetylcholinesterase/1ea5_279_84/1'>Trp 279 and Tyr 121 dominate the peripheral site, and Trp 84 and Phe 330 the active site, together with His 440. </scene> (These numbers are the sequential numbering | help attract and bind the basic, positively charged acetylcholine substrate, although are are some acidic residues nearby. Instead, bulky aromatic residues <scene name='Acetylcholinesterase/1ea5_279_84/1'>Trp 279 and Tyr 121 dominate the peripheral site, and Trp 84 and Phe 330 the active site, together with His 440. </scene> (These numbers are the sequential numbering | ||
of the residues, starting from the N-terminus, according to the '''Torpedo Californica''' form of the enzyme.) | of the residues, starting from the N-terminus, according to the '''Torpedo Californica''' form of the enzyme.) | ||
Most acetylcholinesterases have a net negative charge and a large patch of negative potential around the entrance to the active site gorge, which may be usefull to attract the positively charged acetycholine substrate to the site. As one travels down the gorge, this potential becomes increasingly more and more negative, reaching a peak at the active site at the base. Because of this potential, the peripherial site is thought to act like a substrate trap, that | |||
==Selected structures== | ==Selected structures== | ||
