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Plant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivity


Abstract Butyrylcholinesterase (BChE) is an enzyme with broad substrate and ligand specificities and may function as a generalized bioscavenger by binding and/or hydrolyzing various xenobiotic agents and toxicants, many of which target the central and peripheral nervous systems. Variants of BChE were rationally designed to increase the enzyme’s ability to hydrolyze the psychoactive enantiomer of cocaine. These variants were cloned, and then expressed using the magnICON transient expression system in plants and their enzymatic properties were investigated. In particular, we explored the effects that these site-directed mutations have over the enzyme kinetics with various substrates of BChE. We further compared the affinity of various anticholinestera... (more)
Created Date 2017-09-05
Contributor Larrimore, Katherine (ASU author) / Kazan, I. Can (ASU author) / Kannan, Latha (ASU author) / Kendle, R. Player (ASU author) / Jamal, Tameem (ASU author) / Barcus, Matthew (ASU author) / Bolia, Ashini (ASU author) / Brimijoin, Stephen (Author) / Zhan, Chang-Guo (Author) / Ozkan, Sefika (ASU author) / Mor, Tsafrir (ASU author) / College of Liberal Arts and Sciences / School of Life Sciences / Biodesign Institute / Immunotherapy, Vaccines and Virotherapy / Department of Physics / Center for Biological Physics
Series SCIENTIFIC REPORTS
Type Text
Extent 14 pages
Language English
Identifier DOI: 10.1038/s41598-017-10571-z / ISSN: 2045-2322
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Citation Larrimore, K. E., Kazan, I. C., Kannan, L., Kendle, R. P., Jamal, T., Barcus, M., . . . Mor, T. S. (2017). Plant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivity. Scientific Reports, 7. doi:10.1038/s41598-017-10571-z
Note The final version of this article, as published in Scientific Reports, can be viewed online at: http://www.nature.com/articles/s41598-017-10571-z
Collaborating Institutions ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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