Ontology highlight
ABSTRACT:
SUBMITTER: Flieger A
PROVIDER: S-EPMC95111 | biostudies-literature | 2001 Mar
REPOSITORIES: biostudies-literature
Flieger A A Gong S S Faigle M M Stevanovic S S Cianciotto N P NP Neumeister B B
Journal of bacteriology 20010301 6
We show that Legionella pneumophila possesses lysophospholipase A activity, which releases fatty acids from lysophosphatidylcholine. The NH2-terminal sequence of the enzyme contained FGDSLS, corresponding to a catalytic domain in a recently described group of lipolytic enzymes. Culture supernatants of a L. pneumophila pilD mutant lost the ability to cleave lysophosphatidylcholine. ...[more]