高等学校化学学报 ›› 1998, Vol. 19 ›› Issue (S1): 385.

• Physical Organic Chemistry • 上一篇    下一篇

CAGED CHOLINERGIC LIGANDS AND PHOTOREGULATION OF CHOLINESTERASE ACTIVITIES

Ling Peng, Maurice Goeldner   

  1. Laboratoire de Chimie Bio-organique, URA 1386 CNRS-Facult & #233;de Pharmacie, Universite Louis Pasteur Strasbourg, B. P. 24, F-67401 Illkirch cedex, France
  • 出版日期:1998-12-31 发布日期:1998-12-31

CAGED CHOLINERGIC LIGANDS AND PHOTOREGULATION OF CHOLINESTERASE ACTIVITIES

Ling Peng, Maurice Goeldner   

  1. Laboratoire de Chimie Bio-organique, URA 1386 CNRS-Facult & #233;de Pharmacie, Universite Louis Pasteur Strasbourg, B. P. 24, F-67401 Illkirch cedex, France
  • Online:1998-12-31 Published:1998-12-31

摘要: Photolabile precursors of biologically interesting molecules, or "caged" compounds can provide control of temporal and spatial release of desired molecules by rapid photolysis, and are thus important tools in the study of fast biological processes. Acetylcholinesterase (AChE) is a particularly fast enzynie which hydrolyses the neurotransmitter acetylcholine with a turnover number approaching 20000 s-1. Knowledge of the 3-D structure of AChE[1] has permitted a better understanding of structure-function relationships in the cholinesterases, but has also raised cogent new questions concerning the traffic of substrate and products to and from the active site. Time-resolved crystallography would present an ideal approach to investigate this issue at the atomic level and in real time,provided that suitable probes, which regulate the enzymatic activity by temporally and spatially controled release of enzyme substrates or product.

Abstract: Photolabile precursors of biologically interesting molecules, or "caged" compounds can provide control of temporal and spatial release of desired molecules by rapid photolysis, and are thus important tools in the study of fast biological processes. Acetylcholinesterase (AChE) is a particularly fast enzynie which hydrolyses the neurotransmitter acetylcholine with a turnover number approaching 20000 s-1. Knowledge of the 3-D structure of AChE[1] has permitted a better understanding of structure-function relationships in the cholinesterases, but has also raised cogent new questions concerning the traffic of substrate and products to and from the active site. Time-resolved crystallography would present an ideal approach to investigate this issue at the atomic level and in real time,provided that suitable probes, which regulate the enzymatic activity by temporally and spatially controled release of enzyme substrates or product.

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