Tetanus and botulism neurotoxins: a new group of zinc proteases

Trends Biochem Sci. 1993 Sep;18(9):324-7. doi: 10.1016/0968-0004(93)90065-u.

Abstract

The active forms of tetanus and botulinum neurotoxins, released from the precursor molecule by specific proteolysis and reduction, block the release of neurotransmitters via a Zn(2+)-dependent protease activity. VAMP/synaptobrevin, an integral membrane protein of the synaptic vesicles, is cleaved at a single site by tetanus and botulinum B, D and F neurotoxins. The unique sequence, mechanism of activation and site of activity of clostridial neurotoxins mark them out as an independent group of Zn(2+)-endopeptidases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Botulinum Toxins / metabolism*
  • Humans
  • Membrane Proteins / metabolism
  • Metalloendopeptidases / metabolism
  • Nerve Tissue Proteins / metabolism
  • Nervous System / metabolism
  • Neurotransmitter Agents / metabolism
  • R-SNARE Proteins
  • Tetanus Toxin / metabolism

Substances

  • Membrane Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • R-SNARE Proteins
  • Tetanus Toxin
  • Metalloendopeptidases
  • zinc-endopeptidase, tetanus neurotoxin
  • Botulinum Toxins

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