KEGG ENZYME: 3.4.24.69

ENZYME: 3.4.24.69

Entry

EC 3.4.24.69                Enzyme

Name

bontoxilysin;
botulinum neurotoxin;
BoNT

Class

Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases

Reaction(IUBMB)

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

Comment

This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus [1-5]. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family)

History

EC 3.4.24.69 created 1995

Orthology

K06011

botulinum neurotoxin

Genes

CBO:	CBO0806(botA)

CBA:	CLB_0848(botA)

CBH:	CLC_0862(boNT_A1)

CBY:	CLM_0897(botA)

CBL:	CLK_A0076(botA)

CBK:	CLL_0038(botA)

CBB:	CLD_A0068(botA)

CBI:	CLJ_0004(boNT_BvA4) CLJ_0133(boNT_BvB)

CBN:

CbC4_4096

CBT:	CLH_1110(botA)

CBF:	CLI_0851(boNT_F)

CBM:	CBF_0821(boNT_F)

CBJ:	H04402_00864(cntA_A5)

CBV:	U729_701(botF)

CARG:

RSJ17_00465

» show all

Reference

1 [PMID:8226912]

Authors

Schiavo G, Rossetto O, Catsicas S, Polverino de Laureto P, DasGupta BR, Benfenati F, Montecucco C.

Title

Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D, and E.

Journal

J Biol Chem 268:23784-7 (1993)

Reference

2 [PMID:8243676]

Authors

Schiavo G, Santucci A, Dasgupta BR, Mehta PP, Jontes J, Benfenati F, Wilson MC, Montecucco C

Title

Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds.

Journal

FEBS Lett 335:99-103 (1993)
DOI:10.1016/0014-5793(93)80448-4

Sequence

[ag:CAA43999]

Reference

3 [PMID:8505288]

Authors

Schiavo G, Shone CC, Rossetto O, Alexander FC, Montecucco C.

Title

Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin.

Journal

J Biol Chem 268:11516-9 (1993)

Reference

4 [PMID:8051110]

Authors

Schiavo G, Malizio C, Trimble WS, Polverino de Laureto P, Milan G, Sugiyama H, Johnson EA, Montecucco C.

Title

Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond.

Journal

J Biol Chem 269:20213-6 (1994)

Reference

5 [PMID:7527117]

Authors

Montecucco C, Schiavo G.

Title

Mechanism of action of tetanus and botulinum neurotoxins.

Journal

Mol Microbiol 13:1-8 (1994)
DOI:10.1111/j.1365-2958.1994.tb00396.x

Reference

6 [PMID:7674951]

Authors

Schiavo G, Montecucco C.

Title

Tetanus and botulism neurotoxins: isolation and assay.

Journal

Methods Enzymol 248:643-52 (1995)
DOI:10.1016/0076-6879(95)48041-2

Other DBs

ExplorEnz - The Enzyme Database:

3.4.24.69

IUBMB Enzyme Nomenclature:

3.4.24.69

ExPASy - ENZYME nomenclature database:

3.4.24.69

BRENDA, the Enzyme Database:

3.4.24.69

CAS:	107231-12-9

DBGET integrated database retrieval system