Kinetic analysis of two mutations within Pseudomonas aeruginosa exoenzyme S
(ExoS) showed that a E379D mutation inhibited expression of ADP-ribosyltra
nsferase activity but had little effect on the expression of NAD glycohydro
lase activity while a E381D mutation inhibited expression of both activitie
s. These data identify ExoS as a biglutamic acid ADP-ribosyltransferase, wh
ere E381 is the catalytic residue and E379 contributes to the transfer of A
DP-ribose to the target protein.