3.4.24.69: bontoxilysin
This is an abbreviated version!
For detailed information about bontoxilysin, go to the full flat file.
Reaction
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates
=
Synonyms
abobotulinumtoxinA, antigen E, Balc424, BoNT, BoNT A, BoNT B, BoNT E, BoNT F, BoNT F/A, BoNT LC, BoNT LC/A, BoNT serotype A, BoNT serotype E, BoNT serotype F, BoNT-A, BoNT-C, BoNT-D, BoNT-E, BoNT-F, BoNT/A, BoNT/A LC, BoNT/A Lc endopeptidase, BoNT/A-LC, BoNT/A1, BoNT/A2, BoNT/A3, BoNT/A4, BoNT/A5, BoNT/A6, BoNT/A8, BoNT/B, BoNT/B light chain protease, BoNT/B-LC, BoNT/B1, BoNT/B6, BoNT/C, BoNT/C1, BoNT/C1-LC, BoNT/C3, BoNT/CD, BoNT/D, BoNT/E, BoNT/F, BoNT/F proteolytic F toxin, BoNT/F-LC, BoNT/F1, BoNT/F5, BoNT/F6, BoNT/F7, BoNT/F9, BoNT/FA, BoNT/G, BoNT/HA, BoNT/T, BoNT/X, BoNTA, BoNTA endopeptidase, BoNTB, BoNTC, BoNTE, BoNTF, Bontoxilysin C1, botox A, botulinum A neurotoxin light chain, Botulinum neurotoxin, botulinum neurotoxin a, botulinum neurotoxin A light chain, botulinum neurotoxin A protease, botulinum neurotoxin A subtype 1, botulinum neurotoxin A subtype 2, botulinum neurotoxin A subtype 6, botulinum neurotoxin A3, botulinum neurotoxin A4, botulinum neurotoxin A8 subtype, botulinum neurotoxin B, botulinum neurotoxin B protease, botulinum neurotoxin C, botulinum neurotoxin D light chain, botulinum neurotoxin E, botulinum neurotoxin endopeptidase, botulinum neurotoxin F, botulinum neurotoxin serotype A, botulinum neurotoxin serotype A endopeptidase, botulinum neurotoxin serotype A light chain, botulinum neurotoxin serotype A protease, botulinum neurotoxin serotype B, botulinum neurotoxin serotype BA, botulinum neurotoxin serotype C1, botulinum neurotoxin serotype C1 light chain protease, botulinum neurotoxin serotype D, botulinum neurotoxin serotype E, botulinum neurotoxin serotype F, botulinum neurotoxin serotype FA, botulinum neurotoxin serotype G, botulinum neurotoxin serotype H, botulinum neurotoxin subtype A, botulinum neurotoxin subtype A3, botulinum neurotoxin subtype A4, botulinum neurotoxin subtype B6, botulinum neurotoxin subtype F5, botulinum neurotoxin type A, botulinum neurotoxin type A light chain, botulinum neurotoxin type B, botulinum neurotoxin type C, botulinum neurotoxin type D, botulinum neurotoxin type E, botulinum neurotoxin type F, botulinum neurotoxin type F light chain, botulinum neurotoxin type G, botulinum neurotoxin type HA, botulinum neurotoxin X, Botulinum neurotoxin-A, botulinum toxin, botulinum toxin C3, botulinum toxin serotype E, botulinum toxin serotype F, botulinum toxin type A, botulinum toxin type B, botulinum toxin type F, Botulinumtoxin A, BoTxA, C2 toxin, CDC69016, Clostridium botulinum A2 neurotoxin, Clostridium botulinum C2 toxin, Clostridium botulinum neurotoxin, Clostridium botulinum neurotoxin A1, Clostridium botulinum neurotoxin F, Clostridium botulinum neurotoxin serotype A, Clostridium botulinum neurotoxin serotype A light chain, Clostridium botulinum neurotoxin type E, Clostridium botulinum serotype D neurotoxin, CNT endopeptidase, D-4947 L-TC, daxibotulinumtoxinA, HCB, HCE, incobotulinumtoxinA, LC/A, LC/D, LC/F5, LC/HA, LC/X, LCA, LcB, lcc1, LCD, LCE, LCF, LHn/D, More, mosaic toxin, neurotoxin A, NT, onabotulinumtoxinA, serotype D botulinum neurotoxin, subtype A4 neurotoxin, TeNT, Tetanus neurotoxin, type A BoNT, type A botulinum neurotoxin, type A botulinum neurotoxin light chain, type A botulinum neurotoxin protease, type F toxin
ECTree
Subunits
Subunits on EC 3.4.24.69 - bontoxilysin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
oligomer
oligomerization of BoNT/E is dependent only on GT1b and does not require low pH
?
-
x * 150000, SDS-PAGE
?
x * 146000, recombinant His-tagged BoNT AE and EA chimeras, SDS-PAGE
?
P10845
x * 50000, type A botulinum neurotoxin light chain, SDS-PAGE
?
-
x * 100000 + x * 50000, heavy chain and light chain, SDS-PAGE
?
-
x * 100700 + x * 48800, SDS-PAGE
?
-
x * 49000, botulinum neurotoxin type F light chain, SDS-PAGE
?
x * 50000, light chain subunit of botulinum neurotoxin B, SDS-PAGE
?
-
x * 52200, light chain subunit of botulinum neurotoxin type A, SDS-PAGE
?
-
x * 150000, SDS-PAGE
-
?
-
x * 100000 + x * 50000, heavy chain and light chain, SDS-PAGE
-
?
-
x * 100700 + x * 48800, SDS-PAGE
-
dimer
-
1 * 50000 + 1 * 102000, Clostridium botulinum, serotype BoNT/E, calculated from amino acid sequence, 1 * 51000 + 1 * 104000, Clostridium botulinum, serotype BoNT/B, calculated from amino acid sequence, 1 * 53000 + 1 * 97000, Clostridium botulinum, serotype BoNT/A, calculated from amino acid sequence
dimer
1 * 50000 + 1 * 100000, light chain and heavy chain yielded by posttranslational modification by bacterial or exogenous proteases
dimer
-
1 * 50000 + 1 * 100000, light chain LC and heavy chain HC, linked by a disulfide bridge
dimer
-
1 * 50000 + 1 * 100000, light chain and heavy chain, covalently linked by a disulfide bond
dimer
P10845
1 * 50000, light chain, + 1 * 100000, heavy chain, linked by a disulfide bond
dimer
-
1 * 50000 + 1 * 100000, light chain and heavy chain yielded by posttranslational modification by bacterial or exogenous proteases
-
heterodimer
-
1 * 100000 + 1 * 50000
heterodimer
1 * 100000 + 1 * 50000, SDS-PAGE
heterodimer
P10845
1 * 100000 + 1 * 50000, SDS-PAGE
heterodimer
1 * 100000 + 1 * 50000, SDS-PAGE
heterodimer
1 * 100000 + 1 * 50000, SDS-PAGE
heterodimer
1 * about 100000 + 1 * about 60000, subtype BoNT/F7, SDS-PAGE
heterodimer
1 * about 100000 + 1 * about 70000, subtype BoNT/F5, SDS-PAGE
heterodimer
-
1 * 100000 + 1 * 50000, SDS-PAGE
-
heterodimer
-
1 * 100000 + 1 * 50000, SDS-PAGE
-
additional information
-
each BoNT serotype consists of a heavy chain, HC, of 100 kDa covalently attached by a disulfide bond to a light chain, LC, of 50 kDa
additional information
-
synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds
additional information
-
synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds
additional information
-
synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds
additional information
-
serotype BoNT/E: single-chain polypeptide, serotype BoNT/B: mixture of single- and 2-chain molecules, serotype BoNT/A: 2-chain molecule
additional information
-
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
additional information
-
comparison of wild-type and mutant tertiary structure by circular dichroism, overview
additional information
near-complete conversion of the SC to a disulfide-linked DCas revealed by the appearance of the HC and LC upon SDS-PAGE in the presence of DTT
additional information
-
the enzyme is a binary toxin, which is composed of two separate proteins, the enzyme component C2I and the component C2IIa, overview
additional information
-
BoNT is a 150 kDa protein consisting of a 100 kDa heavy-chain, Hc, and a 50 kDa light-chain, Lc. Epitope mapping of the light chain, overview
additional information
-
BoNT is a modular enzyme of trimodular protein architecture with an N-terminal Zn2+-metalloprotease, which cleaves the SNARE substrate and chaperones the protease across endosomes, and a C-terminal receptor binding module, consisting of two subdomains that determine target specificity by binding to a ganglioside and a protein receptor on the cell surface and triggering endocytosis, overview. The activated mature toxin consists of the three modules: the N-terminal LC Zn2+-metalloprotease, the heavy chain that encompasses the N-terminal translocation domain HN, and the C-terminal receptor-binding domain HC. The latter comprises two subdomains, a beta-sheet jelly roll fold, denoted HCN, and a beta-tree foil fold carboxy subdomain, known as HCC, structure, overview
additional information
-
BoNT/A is composed of a heavy (HC) and light (LC) chain linked by a disulfide bond
additional information
BoNTs are large neurotoxic proteins of about 150 kDa that consist of a light chain of 50 kDa, and a heavy chain of 100 kDa linked by a disulfide bond. BoNTs possess binding, translocation and catalytic domains
additional information
-
BoNTs are large neurotoxic proteins of about 150 kDa that consist of a light chain of 50 kDa, and a heavy chain of 100 kDa linked by a disulfide bond. BoNTs possess binding, translocation and catalytic domains
additional information
-
BoNTs are proteins comprised of three functional domains, the light chains, LCs, the heavy chain, HC, and the translocation HN of the LC into the cell cytoplasm
additional information
-
BoNTs are synthesized as150-kDa proteins consisting of a 100-kDa heavy chain, HC, and a 50-kDa light chain, LC, linked by disulfide bonds
additional information
-
BoNTs consist of a light chain of 50 kDa and a heavy chain of 100 kDa
additional information
-
each BoNT serotype consists of a heavy chain, HC, of 100 kDa covalently attached by a disulfide bond to a light chain, LC, of 50 kDa
additional information
-
each toxin is composed of a heavy, HC, 100 kDa, and a light chain, L, 50 kDa, linked by a disulfide bond and non-covalent interactions
additional information
enzyme model with light chain LC or effector domain, showing the catalytic activity, heavy chain HC binding domain binding to neuronal receptors, after which the HN translocation domain mediates the entry of the light chain into the nerve cell
additional information
P10845
enzyme model with light chain LC or effector domain, showing the catalytic activity, heavy chain HC binding domain binding to neuronal receptors, after which the HN translocation domain mediates the entry of the light chain into the nerve cell
additional information
in BoNT E, both the binding domain and the catalytic domain are on the same side of the translocation domain, and all three have mutual interfaces. This unique association may have an effect on the rate of translocation, with the molecule strategically positioned in the vesicle for quick entry into cytosol. Separation of the domains causes conformational changes. Domain organization of BoNT E, modelling, overview
additional information
-
in BoNT E, both the binding domain and the catalytic domain are on the same side of the translocation domain, and all three have mutual interfaces. This unique association may have an effect on the rate of translocation, with the molecule strategically positioned in the vesicle for quick entry into cytosol. Separation of the domains causes conformational changes. Domain organization of BoNT E, modelling, overview
additional information
-
localization of the antigenic regions on the heavy chains of BoNTs A and B, epitope mapping, overview. Mapping of the regions on BoNTs A and B that bind blocking antibodies in hyperimmune sera against the correlated toxin from human, mouse and other species, submolecular specificity of blocking antibodies that appear in humans, profile and threedimensional structure, overview
additional information
structure comparisons of BoNT/G HCR, BoNT/A HCR, and BoNT/B HCR, modelling, overview
additional information
-
the BoNT HC-LC subunits are held together by a single disulfide bond
additional information
-
the BoNT toxin is composed of a catalytic light chain, a heavy chain, and a translocation domain
additional information
-
the transmembrane domain comprises residues A449 to I873, and the receptor binding domain residues I874 to L1296. Epitope tagging by specific antibodies, recombinant peptide fragment binding experiments, the epitopes for antibodies F1-2 and F1-5 are located between amino acids R564 and S793 on the toxin heavy chain, overview
additional information
-
three-dimensional structure of BoNT showing the catalytic, translocation, and receptor-binding domains, overview
additional information
-
the transmembrane domain comprises residues A449 to I873, and the receptor binding domain residues I874 to L1296. Epitope tagging by specific antibodies, recombinant peptide fragment binding experiments, the epitopes for antibodies F1-2 and F1-5 are located between amino acids R564 and S793 on the toxin heavy chain, overview
-
additional information
-
each BoNT serotype consists of a heavy chain, HC, of 100 kDa covalently attached by a disulfide bond to a light chain, LC, of 50 kDa
additional information
-
synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds