Identification of the catalytic site of clostridial ADP-ribosyltransferases.
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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Institut für Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D003013:Clostridium / Q000201:enzymology*; D008969:Molecular Sequence Data; D011065:Poly(ADP-ribose) Polymerases / Q000235:genetics / Q000378:metabolism*
D011065:Poly(ADP-ribose) Polymerases