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Butyrylcholinesterase-Mediated Enhancement of the Enzymatic Activity of Trypsin

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Abstract

1. Acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BuChE, EC 3.1.1.8) are enzymes that catalyze the hydrolysis of esters of choline.

2. Both AChE and BuChE have been shown to copurify with peptidases.

3. BuChE has also been shown to copurify with other proteins such as transferrin, with which it forms a stable complex. In addition, BuChE is found in association with β-amyloid protein in Alzheimer brain tissues.

4. Since BuChE copurifies with peptidases, we hypothesized that BuChE interacts with these enzymes and that this association had an influence on their catalytic activities. One of the peptidases that copurifies with cholinesterases has specificity similar to trypsin, hence, this enzyme was used as a model to test this hypothesis.

5. Purified BuChE causes a concentration-dependent enhancement of the catalytic activity of trypsin while trypsin does not influence the catalytic activity of BuChE.

6. We suggest that, in addition to its esterase activity, BuChE may assume a regulatory role by interacting with other proteins.

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Authors and Affiliations

  1. Department of Medicine (Neurology and Geriatric Medicine), Halifax, Nova Scotia, Canada

    Sultan Darvesh

  2. Department of Anatomy and Neurobiology, Dalhousie University, Halifax, Nova Scotia, Canada

    Sultan Darvesh & Rohit Kumar

  3. Department of Chemistry, Mount Saint Vincent University, Halifax, Nova Scotia, Canada

    Sultan Darvesh, Sheila Roberts, Ryan Walsh & Earl Martin

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Darvesh, S., Kumar, R., Roberts, S. et al. Butyrylcholinesterase-Mediated Enhancement of the Enzymatic Activity of Trypsin. Cell Mol Neurobiol 21, 285–296 (2001). https://doi.org/10.1023/A:1010947205224

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