Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity

被引：26

作者：

Wictome, M

Rossetto, O

Montecucco, C

Shone, CC

机构：

[1] CTR APPL MICROBIOL & RES,SALISBURY SP4 0JQ,WILTS,ENGLAND

[2] UNIV PADUA,DIPARTIMENTO SCI BIOMED,PADUA,ITALY

来源：

FEBS LETTERS | 1996年 / 386卷 / 2-3期

关键词：

botulinum; neurotoxin; VAMP; synaptobrevin; zinc-endopeptidase; peptide substrate;

D O I：

10.1016/0014-5793(96)00431-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Clostridium botulinum type Il neurotoxin is a highly specific zinc-endopeptidase which cleaves vesicle-associated membrane protein (VAMP/snaptobrevin), a critical component of the vesicle docking/fusion mechanism, In this study, substrate residues flanking the N-terminal side of the cleavage site are shown to play a key role in enzyme substrate recognition, Two aspartate residues in this region are identified as critical determinants of the neurotoxin's specificity, These findings are discussed in relation to the mechanism by which botulinum type B neurotoxin cleaves its substrate.

引用

页码：133 / 136

页数：4

共 16 条

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SHONE, CC
ROBERTS, AK
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1994, 225 (01): : 263 - 270
[2] Role of the disulfide cleavage induced molten globule state of type A botulinum neurotoxin in its endopeptidase activity
Cai, SW
Singh, BR
BIOCHEMISTRY, 2001, 40 (50) : 15327 - 15333
[3] Identification of Residues Surrounding the Active Site of Type A Botulinum Neurotoxin Important for Substrate Recognition and Catalytic Activity
S. Ashraf Ahmed
Mark A. Olson
Matthew L. Ludivico
Janice Gilsdorf
Leonard A. Smith
The Protein Journal, 2008, 27 : 151 - 162
[4] Identification of residues surrounding the active site of type a botulinum neurotoxin important for substrate recognition and catalytic activity
Ahmed, S. Ashraf
Olson, Mark A.
Ludivico, Matthew L.
Gilsdorf, Janice
Smith, Leonard A.
PROTEIN JOURNAL, 2008, 27 (03): : 151 - 162
[5] Comparative endopeptidase activity of Clostridium botulinum Type B Neurotoxin Complex and Recombinant Type B light Chain to explore the role of neurotoxin associated proteins in active enzyme structure
Riding, S
Lindo, P
Biegel, E
Singh, BR
FASEB JOURNAL, 2004, 18 (08): : C141 - C141
[6] Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III
Conrad, C
Evguenieva-Hackenberg, E
Klug, G
FEBS LETTERS, 2001, 509 (01) : 53 - 58
[7] Analysis of amino acid residues in the N-terminal region of the beta-neurotoxin CssII and its specificity for voltage-gated Na+ channel subtypes
Ibarra Vega, Rodrigo
Jimenez Vargas, Juana Maria
Restano Cassulini, Rita
Estrada, Georgina
Possani, Lourival D.
Corzo, Gerardo
NEW BIOTECHNOLOGY, 2014, 31 : S201 - S201
[8] A PEPTIDASE (AMINOPEPTIDASE B) FROM CAT AND GUINEA PIG LIVER SELECTIVE FOR N-TERMINAL ARGININE AND LYSINE RESIDUES .I. PURIFICATION AND SUBSTRATE SPECIFICITY
HOPSU, VK
MAKINEN, KK
GLENNER, GG
ACTA CHEMICA SCANDINAVICA, 1966, 20 (05): : 1225 - &
[9] Sequence of the gene for Clostridium botulinum type B neurotoxin associated with infant botulism, expression of the C-terminal half of heavy chain and its binding activity
Ihara, H
Kohda, T
Morimoto, F
Tsukamoto, K
Karasawa, T
Nakamura, S
Mukamoto, M
Kozaki, S
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 2003, 1625 (01): : 19 - 26
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Kohda, Tomoko
Ihara, Hideshi
Seto, Yukiji
Tsutsuki, Hiroyasu
Mukamoto, Masafumi
Kozaki, Shunji
MICROBIAL PATHOGENESIS, 2007, 42 (2-3) : 72 - 79

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