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Literature summary for 3.4.24.69 extracted from

  • Chen, S.; Kim, J.J.; Barbieri, J.T.
    Mechanism of substrate recognition by botulinum neurotoxin serotype A (2007), J. Biol. Chem., 282, 9621-9627.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C134A site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
D370A site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
D370R site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
E257A site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
E257K site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
F163A site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
F194A site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
F194A/T220A site-directed mutagenesis, mutation of S1' pocket residues, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
H269A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Clostridium botulinum
I115A site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
K41A site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
L175A site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
L175A/R177A site-directed mutagenesis, mutation of S5 pocket residues, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
Q162A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Clostridium botulinum
R177A site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
T176A site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
T220A site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum
V129A site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme Clostridium botulinum

Inhibitors

Inhibitors Comment Organism Structure
L-Arginine hydroxamate
-
Clostridium botulinum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0083
-
SNAP25 pH 7.6, 37°C, recombinant mutant L175A/R177A Clostridium botulinum
0.009
-
SNAP25 pH 7.6, 37°C, recombinant mutant F194A Clostridium botulinum
0.0092
-
SNAP25 pH 7.6, 37°C, recombinant mutant F194A/T220A Clostridium botulinum
0.011
-
SNAP25 pH 7.6, 37°C, recombinant mutant D370R Clostridium botulinum
0.011
-
SNAP25 pH 7.6, 37°C, recombinant mutant L175A Clostridium botulinum
0.012
-
SNAP25 pH 7.6, 37°C, recombinant mutant F163A Clostridium botulinum
0.012
-
SNAP25 pH 7.6, 37°C, recombinant mutant R177A Clostridium botulinum
0.014
-
SNAP25 pH 7.6, 37°C, recombinant mutant D370A Clostridium botulinum
0.014
-
SNAP25 pH 7.6, 37°C, recombinant mutant T176A Clostridium botulinum
0.016
-
SNAP25 pH 7.6, 37°C, recombinant wild-type enzyme Clostridium botulinum
0.016
-
SNAP25 pH 7.6, 37°C, recombinant mutant H269A Clostridium botulinum
0.017
-
SNAP25 pH 7.6, 37°C, recombinant mutant Q162A Clostridium botulinum
0.019
-
SNAP25 pH 7.6, 37°C, recombinant mutant E257A Clostridium botulinum
0.02
-
SNAP25 pH 7.6, 37°C, recombinant mutant T220A Clostridium botulinum
0.027
-
SNAP25 pH 7.6, 37°C, recombinant mutant E257K Clostridium botulinum
0.053
-
SNAP25 pH 7.6, 37°C, recombinant mutant V129A Clostridium botulinum
0.061
-
SNAP25 pH 7.6, 37°C, recombinant mutant C134A Clostridium botulinum
0.095
-
SNAP25 pH 7.6, 37°C, recombinant mutant I115A Clostridium botulinum
0.098
-
SNAP25 pH 7.6, 37°C, recombinant mutant K41A Clostridium botulinum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SNAP25 + H2O Clostridium botulinum i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, the enzyme cleaves SNARE proteins, i.e. SNAP receptor proteins, to elicit flaccid paralysis by inhibiting neurotransmitter-carrying vesicle fusion to the plasma membrane of peripheral neurons, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SNAP25 + H2O i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, the enzyme cleaves SNARE proteins, i.e. SNAP receptor proteins, to elicit flaccid paralysis by inhibiting neurotransmitter-carrying vesicle fusion to the plasma membrane of peripheral neurons, overview Clostridium botulinum ?
-
?
SNAP25 + H2O i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, recombinant GST-tagged wild-type and mutant D193A, R198A, R198E, and I171A substrates, full-length and truncated substrate, SNAP25 initially binds along the belt region of BoNT/A, which aligns the P5 residue to the S5 pocket at the periphery of the active site, binding site structures, reaction mechanism, molecular modeling of the LC/A active site domain, overview Clostridium botulinum ?
-
?

Synonyms

Synonyms Comment Organism
BoNT/A
-
Clostridium botulinum
botulinum neurotoxin serotype A
-
Clostridium botulinum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Clostridium botulinum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
SNAP25 pH 7.6, 37°C, recombinant mutant D370R Clostridium botulinum
0.1
-
SNAP25 pH 7.6, 37°C, recombinant mutant D370A Clostridium botulinum
0.1
-
SNAP25 pH 7.6, 37°C, recombinant mutant E257K Clostridium botulinum
0.19
-
SNAP25 pH 7.6, 37°C, recombinant mutant F194A/T220A Clostridium botulinum
0.2
-
SNAP25 pH 7.6, 37°C, recombinant mutant F194A Clostridium botulinum
0.3
-
SNAP25 pH 7.6, 37°C, recombinant mutant T220A Clostridium botulinum
0.4
-
SNAP25 pH 7.6, 37°C, recombinant mutant F163A Clostridium botulinum
0.7
-
SNAP25 pH 7.6, 37°C, recombinant mutant L175A Clostridium botulinum
0.8
-
SNAP25 pH 7.6, 37°C, recombinant mutant L175A/R177A Clostridium botulinum
1.1
-
SNAP25 pH 7.6, 37°C, recombinant mutants R177A and E257A Clostridium botulinum
1.2
-
SNAP25 pH 7.6, 37°C, recombinant mutant T176A Clostridium botulinum
11
-
SNAP25 pH 7.6, 37°C, recombinant mutants I115A and C134A Clostridium botulinum
12
-
SNAP25 pH 7.6, 37°C, recombinant mutants K41A and V129A Clostridium botulinum
58
-
SNAP25 pH 7.6, 37°C, recombinant mutant H269A Clostridium botulinum
60
-
SNAP25 pH 7.6, 37°C, recombinant wild-type enzyme Clostridium botulinum
63
-
SNAP25 pH 7.6, 37°C, recombinant mutant Q162A Clostridium botulinum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Clostridium botulinum