Information on EC 3.4.24.69 - bontoxilysin

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The expected taxonomic range for this enzyme is: Clostridium

EC NUMBER
COMMENTARY hide
3.4.24.69
-
RECOMMENDED NAME
GeneOntology No.
bontoxilysin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
107231-12-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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G7BEA8
UniProt
Manually annotated by BRENDA team
Clostridium botulinum BoNT/C BoNT/D
BoNT/C, BoNT/D
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Manually annotated by BRENDA team
BoNT/E
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain CB16
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Clostridium botulinum Hall A
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UniProt
Manually annotated by BRENDA team
Clostridium botulinum Hall A hyper
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UniProt
Manually annotated by BRENDA team
strain NCTC 11219
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain Stockholm
SwissProt
Manually annotated by BRENDA team
Clostridium botulinum type A
type A
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Manually annotated by BRENDA team
Clostridium botulinum type G
type G strain
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Manually annotated by BRENDA team
F
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
25-kDa synaptosome-associated protein + H2O
?
show the reaction diagram
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i.e. SNAP-25
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?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-6-aminohexaoic acid-CONH2 + H2O
?
show the reaction diagram
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-
-
-
?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-CONH2 + H2O
?
show the reaction diagram
-
-
-
-
?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-norleucine-CONH2 + H2O
?
show the reaction diagram
-
-
-
-
?
50-mer synaptobrevin peptide + H2O
?
show the reaction diagram
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[Pya88]S39-88
-
?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-6-aminohexaoic acid-CONH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-CONH2 + H2O
?
show the reaction diagram
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-
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?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-norleucine-CONH2 + H2O
?
show the reaction diagram
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-
-
-
?
Ac-ERDQKLSELDDRADALQAG-(7-methoxy-4-methylcoumaryl)Lys-SQ-diaminopropionic acid(2,4-dinitrophenyl)-ESSAAKLKRKYWWKNLK-NH2 + H2O
?
show the reaction diagram
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development of a FRET peptide substrate, based on the native substrate binding site of human VAMP2 residues 55-94, and evaluation for enzymatic cleavage by the BoNT/B light chain protease, overview. For the synthesis position 74 is mutated to Lys in order to couple 7-methoxycoumarin-4-acetic acid, MCA, to the amine via an amide bond, in part to aid in the flexibility of the MCA to allow free rotation away from the active site and not affect binding and/or cleavage of the peptide. At position 77 the native Phe is replaced with the unnatural amino acid diaminopropionic acid to facilitate coupling of 2,4-dinitrophenyl to the peptide. Thr79 is mutated to a serine increasing kcat 2fold without affecting Km
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?
Ac-IIGNLRH(Nle)ALD(Nle)GNEIDTQNRQIDRI(Nle)EKADSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-IIGNLRH(Nle)ALD(Nle)GNEIDTQNRQIDRI(Nle)EKADSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
show the reaction diagram
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i.e. peptide PL51, a SNAP-25-NH2in which all methionines were replaced by nonoxidizable Nle
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?
Ac-IIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-IIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
show the reaction diagram
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i.e. peptide PL50, a SNAP-25-NH2 acetylated at positions 156 to 203 [(pNO2-Phe)197, (1-pyrenylalanine)200, Nle202]
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?
Ac-KSDSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)LGSG-NH2 + H2O
Ac-KSDSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)LGSG-NH2
show the reaction diagram
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-
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?
Ac-RGSNKPKIDAGNQRATRXLGGR-NH2 + H2O
Ac-RGSNKPKIDAGNQR + ATRXLGGR-NH2
show the reaction diagram
Ac-SNKTIDEANQRATKML-NH2 + H2O
Ac-SNKTIDEANQ + RATKML-NH2
show the reaction diagram
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synaptosomal protein
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?
Ac-SNKTRIDCANQRATKML-NH2 + H2O
Ac-SNKTRIDCANQ + RATKML-NH2
show the reaction diagram
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-
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?
Ac-SNKTRIDEAN(1-pyrenylalanine)RA(pNO2-Phe)K(Nle)L-NH2 + H2O
Ac-SNKTRIDEAN(1-pyrenylalanine) + RA(pNO2-Phe)K(Nle)L-NH2
show the reaction diagram
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?
Ac-SNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-SNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
show the reaction diagram
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?
Ac-SNKTRIDEANQRATK(Nle)L-NH2 + H2O
Ac-SNKTRIDEANQ + RATK(Nle)L-NH2
show the reaction diagram
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-
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?
Ac-SNKTRIDEANQRATKML-NH2 + H2O
Ac-SNKTRIDEANQ + RATKML-NH2
show the reaction diagram
-
-
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?
Ac-SNKTRIDEANQRCTKML-NH2 + H2O
Ac-SNKTRIDEANQ + RCTKML-NH2
show the reaction diagram
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-
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?
Ac-SNKTRIDECNQRATKML-NH2 + H2O
Ac-SNKTRIDECNQ + RATKML-NH2
show the reaction diagram
-
-
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?
biotin-KGSNRTRIDQGNQRATRXLGGK-biotin + H2O
?
show the reaction diagram
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the catalytic activity resides on the light chains of the toxin molecule
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?
cytosolic SNARE + H2O
?
show the reaction diagram
LQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDD + H2O
LQQTQAQVDEVVDI + MRVNVDKVLERDQK + LSELDD
show the reaction diagram
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the vesicle-associated membrane protein, VAMP, sequence-derived peptide is a substrate of BoNT serotype D light chain
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?
LSELDDRADALQAGASQFETSAAKLKRKYWWKNLK + H2O
LSELDDRADALQAGASQ + FETSAAKLKRKYWWKNLK
show the reaction diagram
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the vesicle-associated membrane protein, VAMP, sequence-derived peptide is a substrate of BoNT serotype B light chain
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?
membrane-anchored SNARE + H2O
?
show the reaction diagram
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host membrane-anchored SNARE, proteolytically cleaved by BoNT/C
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?
Neuroexocytosis multi-subunit complex + H2O
?
show the reaction diagram
neuronal proteinSNAP-25 + H2O
?
show the reaction diagram
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?
Proteins of neuroexocytosis apparatus + H2O
?
show the reaction diagram
Recombinant glutathione S-methyltransferase VAMP-2 fusion protein + H2O
Hydrolyzed recombinant glutathione S-methyltransferase VAMP-2 fusion protein
show the reaction diagram
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2 proteolytic fragments, MW 36000 and MW 6000
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Sb-Snc2p fusion protein + H2O
?
show the reaction diagram
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a recombinant chimeric SNARE protein where a portion of neuronal synaptobrevin, Sb, is fused to Snc2p, a Sb ortholog required for protein secretion from yeast cells
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?
SNAP-23 + H2O
?
show the reaction diagram
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a nonneuronal SNARE protein, that mediates vesicle-plasma membrane fusion processes, including secretion of airway mucus, antibody, insulin, gastric acids, and ions. SNAP23 is cleaved by an engineered BoNT/E light chain, LC/E K224D. Molecular modeling of the enzyme-substrate complex using the crystal structure of LC/E, Protein Data Bank ID 3d3x, overview
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?
SNAP-25 + H2O
?
show the reaction diagram
SNAP-25 peptide (141-206) + H2O
?
show the reaction diagram
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the minimal size of SNAP-25 known to retain full activity as a BoNT/A substrate is the C-terminal 66-mer peptide, residues 141-206, with both exosites
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?
SNAP-25-derived peptide + H2O
?
show the reaction diagram
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i.e. HA-tagged SNAP25(141-206) or HA-tagged mutant SNAP25(141-206)-R198A, substrate of light chains of BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4
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-
?
SNAP25 + H2O
?
show the reaction diagram
SNAP25(187-203) + H2O
?
show the reaction diagram
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i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, substrate fragmnent containing residues 87-203
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?
SNAPEtide + H2O
?
show the reaction diagram
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substrate for subtype BoNT/E
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?
SNAPtide + H2O
?
show the reaction diagram
SNARE-protein + H2O
?
show the reaction diagram
-
soluble NSF-attachment protein receptor
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?
SNKTRIDEAAQRATKML + H2O
SNKTRIDEAAQ + RATKML
show the reaction diagram
-
synthetic peptide substrate
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?
SNKTRIDEANBRATKML + H2O
SNKTRIDEANB + RATKML
show the reaction diagram
-
synthetic peptide substrate
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?
SNKTRIDEANNRATKML + H2O
SNKTRIDEANN + RATKML
show the reaction diagram
-
synthetic peptide substrate
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?
SNKTRIDEANQRABKML + H2O
SNKTRIDEANQ + RABKML
show the reaction diagram
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synthetic peptide substrate
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?
SNKTRIDEANQRASKML + H2O
SNKTRIDEANQ + RASKML
show the reaction diagram
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synthetic peptide substrate
-
?
SNKTRIDEANQRATAML + H2O
SNKTRIDEANQ + RATAML
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATK + H2O
SNKTRIDEANQ + RATK
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKAL + H2O
SNKTRIDEANQ + RATKAL
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKM + H2O
SNKTRIDEANQ + RATKM
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKML + H2O
SNKTRIDEANQ + RATKML
show the reaction diagram
SNKTRIDEANQRATKXL + H2O
SNKTRIDEANQ + RATKXL
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEANQRBTKML + H2O
SNKTRIDEANQ + RBTKML
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRIDEBNQRATKML + H2O
SNKTRIDEBNQ + RATKML
show the reaction diagram
-
synthetic peptide substrate
-
?
SNKTRINEAAQRATKML + H2O
SNKTRINEAAQ + RATKML
show the reaction diagram
-
synthetic peptide substrate
-
?
SNRTRIDEANK(Dnp)RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML + H2O
SNRTRIDEANK(Dnp) + RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML
show the reaction diagram
synaptobrevin + H2O
?
show the reaction diagram
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
show the reaction diagram
synaptobrevin-2 + H2O
?
show the reaction diagram
Synaptosome-associated protein + H2O
?
show the reaction diagram
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
show the reaction diagram
synaptosome-associated protein SNAP-25 + H2O
?
show the reaction diagram
synaptosome-associated protein SNAP-25 + H2O
hydrolyzed synaptosome-associated protein SNAP-25
show the reaction diagram
-
-
-
-
?
Syntaxin + H2O
?
show the reaction diagram
VAMP + H2O
?
show the reaction diagram
VAMP 2 + H2O
?
show the reaction diagram
VAMP-1 + H2O
?
show the reaction diagram
VAMP-2 + H2O
?
show the reaction diagram
VAMP2 + H2O
?
show the reaction diagram
VAMP2 peptide + H2O
?
show the reaction diagram
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a synthetic peptide substrate representing amino acid residues 60-94 of the intracellular vesicle associated membrane protein 2, i.e. VAMP2, recombinant GST fusion protein and commercial preparation as substrates with equal activity for BONT/B
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?
VAMPTide + H2O
?
show the reaction diagram
vesicle-associated membrane protein VAMP + H2O
?
show the reaction diagram
-
BoNT F cleaves VAMP between residues Q58 and K59. The minimum substrate is a peptide containing VAMP residues 32-65, which includes only one of the two VAMP structural motifs thought to be required for botulinum substrate recognition. BoNT F exhibits a strict requirement for residues D57 (P2), K59 (P1'), and L60 (P2'), but peptides containing substitutions for R56 (P3), Q58 (P1), and S61 (P3') are cleaved. Therefore, the P2, P1', and P2'?residues of VAMP are of paramount importance for BoNT F substrate recognition near the scissile bond
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-
?
vesicle-associated membrane protein VAMP-2 + H2O
?
show the reaction diagram
-
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
25-kDa synaptosome-associated protein + H2O
?
show the reaction diagram
-
i.e. SNAP-25
-
-
?
Ac-SNKTIDEANQRATKML-NH2 + H2O
Ac-SNKTIDEANQ + RATKML-NH2
show the reaction diagram
-
synaptosomal protein
-
?
cytosolic SNARE + H2O
?
show the reaction diagram
-
host cytosolic SNARE, i.e. soluble NSF attachment protein receptor, a central helical protein-conducting channel, which chaperones the protease across host endosomes, modelling, overview. Sequence-specific claveage by the endoprotease activity of the BoNT light chains
-
-
?
membrane-anchored SNARE + H2O
?
show the reaction diagram
-
host membrane-anchored SNARE, proteolytically cleaved by BoNT/C
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
show the reaction diagram
SNAP-25 + H2O
?
show the reaction diagram
SNAP25 + H2O
?
show the reaction diagram
SNARE-protein + H2O
?
show the reaction diagram
-
soluble NSF-attachment protein receptor
-
?
synaptobrevin + H2O
?
show the reaction diagram
Synaptosome-associated protein + H2O
?
show the reaction diagram
synaptosome-associated protein SNAP-25 + H2O
?
show the reaction diagram
-
botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
-
-
?
Syntaxin + H2O
?
show the reaction diagram
VAMP + H2O
?
show the reaction diagram
VAMP 2 + H2O
?
show the reaction diagram
-
i.e. synaptobrevin-2 or vesicle-associated membrane protein 2
-
-
?
VAMP-2 + H2O
?
show the reaction diagram
VAMP2 + H2O
?
show the reaction diagram
vesicle-associated membrane protein-2 + H2O
?
show the reaction diagram
P19321
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-
-
?
additional information
?
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