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Literature summary for 3.4.24.69 extracted from

  • Chen, S.; Hall, C.; Barbieri, J.T.
    Substrate recognition of VAMP-2 by botulinum neurotoxin B and tetanus neurotoxin (2008), J. Biol. Chem., 283, 21153-21159.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information single point mutations in VAMP-2 for analysation of binding kinetics to TeNT Clostridium tetani

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information mutations at residues 41-51 of substrate vesicle-associated membrane protein 2 show dramatic effects on LC/TeNT cleavage with 320-fold inhibition by the individual mutations, E41A, V42A, V43A, and R47A. Deletion of the N-terminal 50 residues of vesicle-associated membrane protein 2 causes a 500-fold reduction in LC/TeNT efficiency. Mutation D44A shows a 10-fold higher Km (46 microM) and 10-fold lower Turnover Number (0.018 1/sec) than wild-type vesicle-associated membrane protein 2 Clostridium tetani

Organism

Organism UniProt Comment Textmining
Clostridium tetani
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mapping experiment shows that residues 40-87 of vesicle-associated membrane protein 2 are sufficient for efficient TeNT cleavage. Mutations in vesicle-associated membrane protein 2 for analysation of binding kinetics to TeNT Clostridium tetani ?
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?

Synonyms

Synonyms Comment Organism
TeNT
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Clostridium tetani
Tetanus neurotoxin
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Clostridium tetani