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Identification of the Catalytic Site of Clostridial ADP-Ribosyltransferases

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ADP-Ribosylation in Animal Tissues

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 419))

Abstract

The catalytic sites of clostridial ADP-ribosyltransferases were studied by photoaffinity-labelling with [carbonyl-14C]NAD+. In C3-like transferases, which are known to modify low molecular mass GTP-binding Rho proteins, Glu-174 was identified to be essential for catalysis. In C. perfringens iota toxin, Glu-380 and Glu-378 may have pivotal roles in the active site of this actin-ADP-ribosylating toxin.

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Authors and Affiliations

  1. Institut für Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Hermann-Herderstr. 5, D-79104, Freiburg, Germany

    Klaus Aktories

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  1. University Hospital Hamburg-Eppendorf, Hamburg, Germany

    Friedrich Haag  & Friedrich Koch-Nolte  & 

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Aktories, K. (1997). Identification of the Catalytic Site of Clostridial ADP-Ribosyltransferases. In: Haag, F., Koch-Nolte, F. (eds) ADP-Ribosylation in Animal Tissues. Advances in Experimental Medicine and Biology, vol 419. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8632-0_6

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  • DOI: https://doi.org/10.1007/978-1-4419-8632-0_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4652-4

  • Online ISBN: 978-1-4419-8632-0

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