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Toxins 2010, 2(5), 978-997; doi:10.3390/toxins2050978

The Zinc-Dependent Protease Activity of the Botulinum Neurotoxins

US Army Medical Research and Materiel Command, Ft. Detrick, MD 21702-5012, USA
Bioinformatics Support Group, Advanced Biomedical Computing Center, Information Systems Program, SAIC-Frederick Inc., NCI-Frederick, Frederick, MD 21702, USA
Botulinum Research Center, University of Massachusetts Dartmouth, 285 Old Westport Road, Dartmouth, MA 02747, USA
US Army Medical Research Institute of Chemical Defense, Aberdeen Proving Ground, MD 21010-5400, USA
Author to whom correspondence should be addressed.
Received: 1 April 2010 / Revised: 30 April 2010 / Accepted: 5 May 2010 / Published: 7 May 2010
(This article belongs to the Special Issue Protein Toxins as Proteases)
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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 (
Keywords: catalysis; energy; kcat; Km; superactivation catalysis; energy; kcat; Km; superactivation
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Lebeda, F.J.; Cer, R.Z.; Mudunuri, U.; Stephens, R.; Singh, B.R.; Adler, M. The Zinc-Dependent Protease Activity of the Botulinum Neurotoxins. Toxins 2010, 2, 978-997.

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