Ontology highlight
ABSTRACT:
SUBMITTER: Radke J
PROVIDER: S-EPMC96488 | biostudies-literature | 1999 Mar
REPOSITORIES: biostudies-literature
Radke J J Pederson K J KJ Barbieri J T JT
Infection and immunity 19990301 3
Kinetic analysis of two mutations within Pseudomonas aeruginosa exoenzyme S (ExoS) showed that a E379D mutation inhibited expression of ADP-ribosyltransferase activity but had little effect on the expression of NAD glycohydrolase activity while a E381D mutation inhibited expression of both activities. These data identify ExoS as a biglutamic acid ADP-ribosyltransferase, where E381 is the catalytic residue and E379 contributes to the transfer of ADP-ribose to the target protein. ...[more]