The zinc-dependent protease activity of the botulinum neurotoxins

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...

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Bibliographic Details
Published inToxins Vol. 2; no. 5; pp. 978 - 997
Main Authors Lebeda, Frank J, Cer, Regina Z, Mudunuri, Uma, Stephens, Robert, Singh, Bal Ram, Adler, Michael
Format Journal Article Book Review
LanguageEnglish
Published Switzerland MDPI AG 01.05.2010
MDPI
Subjects
Botulinum Toxins - chemistry
catalysis
energy
Food contamination
kcat
Kinetics
Neurotoxins
Neurotoxins - antagonists & inhibitors
Neurotoxins - chemistry
Peptide Hydrolases - metabolism
Protein Conformation
Review
SNARE Proteins - metabolism
superactivation
Toxins
Zinc - metabolism
superactivation
catalysis
kcat
Km
energy
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Summary: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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ISSN:2072-6651
2072-6651
DOI:10.3390/toxins2050978