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

FEBS Letters
J van DammeK Aktories

Abstract

The enzyme component of 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-Va l-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 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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Citations

Jun 7, 2003·Advances in Enzyme Regulation·Jun SakuraiHideaki Tsuge
Feb 6, 2013·Proceedings of the National Academy of Sciences of the United States of America·Toshiharu TsurumuraHideaki Tsuge
Mar 29, 2000·Journal of Bacteriology·M NagahamaJ Sakurai
Sep 9, 2004·Microbiology and Molecular Biology Reviews : MMBR·Holger BarthBradley G Stiles
Dec 1, 2009·Toxins·Jun SakuraiKeiko Kobayashi
Jan 8, 2008·International Journal of Laboratory Hematology·S D BoydD A Arber
May 17, 2006·Anaerobe·Klaus Aktories, Holger Barth
Nov 22, 1996·The Journal of Biological Chemistry·N HaraM Shimoyama
Apr 4, 2021·International Journal of Molecular Sciences·Dinendra L AbeyawardhaneDavid J Weber

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