Section 9
Chapter 8,158

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

Van Damme, J.; Jung, M.; Hofmann, F.; Just, I.; Vandekerckhove, J.; Aktories, K.

Febs Letters 380(3): 291-295


ISSN/ISBN: 0014-5793
PMID: 8601443
DOI: 10.1016/0014-5793(96)00052-x
Accession: 008157575

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The enzyme component of the actin ADP-ribosylating Clostridium perfringens iota toxin was affinity labelled by UV irradiation in the presence of (carbonyl-14C)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-Gly-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. perfringens iota toxin.

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