Analysis of the catalytic site of the actin ADP-ribosylating Clostridium perfringens iota toxin

被引：26
|
作者：
vanDamme, J
Jung, M
Hofmann, F
Just, I
Vandekerckhove, J
Aktories, K
机构：
[1] UNIV FREIBURG, INST PHARMAKOL & TOXIKOL, D-79104 FREIBURG, GERMANY
[2] STATE UNIV GHENT, FAC MED, DEPT BIOCHEM, INST BIOTECHNOL, B-9000 GHENT, BELGIUM
[3] UNIV SAARLAND, INST PHARMAKOL & TOXIKOL, D-66421 HOMBURG, GERMANY
来源：
FEBS LETTERS | 1996年 / 380卷 / 03期
关键词：
D O I：
10.1016/0014-5793(96)00052-X
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：
The enzyme component of the actin ADP-rihosylating Clostridium perfringens iota toxin was affinity labelled by UV irradiation in the presence of [carbonyl-C-14]NAD. A peptide containing the radiolabel was generated by CNBr cleavage and subsequent proteolysis with trypsin, Its amino acid sequence is Gly-Ser-Pro-Gly-Ala-Tyr-Leu-Ser-Ala-Ile-Pro-Gly-Tyr-Ala-G-ly-X-Tyr-Glu-Val-Leu-Leu-Asn-His-Gly-Ser-Lys corresponding with the region Gly-363 through Lys-388 in the C. perfringens iota toxin. Mass spectrometric data as well as the results of the PTH-amino acid analysis are in line with a modification of a glutamic acid side chain located at position 378. Therefore, in addition to Glu-380, as could be concluded by analogy with other ADP-ribosyltransferases, Glu-378 may play a pivotal role in the active site of C. peufringens iota toxin.
引用
收藏
页码：291 / 295
页数：5
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