The zinc-dependent protease activity of the botulinum neurotoxins

Toxins (Basel). 2010 May;2(5):978-97. doi: 10.3390/toxins2050978. Epub 2010 May 7.

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).

Keywords: Km; catalysis; energy; kcat; superactivation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Botulinum Toxins / chemistry*
  • Kinetics
  • Neurotoxins / antagonists & inhibitors
  • Neurotoxins / chemistry*
  • Peptide Hydrolases / metabolism*
  • Protein Conformation
  • SNARE Proteins / metabolism
  • Zinc / metabolism*

Substances

  • Neurotoxins
  • SNARE Proteins
  • Peptide Hydrolases
  • Botulinum Toxins
  • Zinc