Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Neumeyer, T.; Schiffler, B.; Maier, E.; Lang, A.E.; Aktories, K.; Benz, R.
    Clostridium botulinum C2 toxin. Identification of the binding site for chloroquine and related compounds and influence of the binding site on properties of the C2II channel (2008), J. Biol. Chem., 283, 3904-3914.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.69 expression of GST-tagged wild-type and mutant C2II components in Escherichia coli strain BL21 Clostridium botulinum

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.69 D341A site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 D342C site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 D426A site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 E272A site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 E280C site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 E346A site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 E399/D426A/F428A site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity Clostridium botulinum
3.4.24.69 E399A site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 E399A/D425A site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity Clostridium botulinum
3.4.24.69 F428A site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 F428D site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 F428W site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme Clostridium botulinum
3.4.24.69 F428Y site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme Clostridium botulinum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.69 Chloroquine the C2II channel can be blocked by chloroquine and related compounds Clostridium botulinum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.69 membrane the C2II binding component forms cation-selective and chloroquine-sensitive heptameric channels into lipid bilayer membranes, which is essential for C2I catalytic component transport into target cells Clostridium botulinum 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.69 additional information the C2II channel is cation-selective Clostridium botulinum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.69 60000
-
 7 * 60000, activated C2II binding component, which oligomerizes into heptamers and forms channels in lipid bilayer membranes, residues 303-330 of C2II contain a conserved pattern of alternating hydrophobic and hydrophilic residues, which is involved in the formation of two amphipathic beta-strands involved in membrane insertion and channel formation Clostridium botulinum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.69 additional information Clostridium botulinum the proteolytically activated 60 kDa C2II binding component is essential for C2I transport into target cells involving especially amino acids Glu399, Asp426, and Phe428, it forms heptameric channels into membranes that are cation-selective and can be blocked by chloroquine and related compounds ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.69 Clostridium botulinum
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.69 proteolytic modification the C2II binding enzyme component is proteolytically activated Clostridium botulinum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.69 recombinant GST-tagged wild-type and mutant C2II components from Escherichia coli strain BL21 Clostridium botulinum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.69 additional information the proteolytically activated 60 kDa C2II binding component is essential for C2I transport into target cells involving especially amino acids Glu399, Asp426, and Phe428, it forms heptameric channels into membranes that are cation-selective and can be blocked by chloroquine and related compounds Clostridium botulinum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.69 heptamer 7 * 60000, activated C2II binding component, which oligomerizes into heptamers and forms channels in lipid bilayer membranes, residues 303-330 of C2II contain a conserved pattern of alternating hydrophobic and hydrophilic residues, which is involved in the formation of two amphipathic beta-strands involved in membrane insertion and channel formation Clostridium botulinum
3.4.24.69 More Clostridium botulinum C2 toxin is a binary AB type toxin that is structurally organized into distinct enzyme and binding components, i.e. A and C2I components and B and C2II components, respectively Clostridium botulinum

Synonyms

EC Number Synonyms Comment Organism
3.4.24.69 Clostridium botulinum C2 toxin
-
 Clostridium botulinum
3.4.24.69 More Clostridium botulinum C2 toxin belongs to the family of binary AB type toxins Clostridium botulinum