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The Zinc-Dependent Protease Activity of the Botulinum Neurotoxins

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Author(s): Frank J. Lebeda | Regina Z. Cer | Uma Mudunuri | Robert Stephens | Bal Ram Singh | Michael Adler

Journal: Toxins
ISSN 2072-6651

Volume: 2;
Issue: 5;
Start page: 978;
Date: 2010;
Original page

Keywords: catalysis | energy | kcat | Km | superactivation

ABSTRACT
The botulinum neurotoxins (BoNT, serotypes A-G) are some of the most toxic proteins known and are the causative agents of botulism. Following exposure, the neurotoxin binds and enters peripheral cholinergic nerve endings and specifically and selectively cleaves one or more SNARE proteins to produce flaccid paralysis. This review centers on the kinetics of the Zn-dependent proteolytic activities of these neurotoxins, and briefly describes inhibitors, activators and factors underlying persistence of toxin action. Some of the structural, enzymatic and inhibitor data that are discussed here are available at the botulinum neurotoxin resource, BotDB (http://botdb.abcc.ncifcrf.gov).
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