Novel lysophospholipase A secreted by Legionella pneumophila.
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.
Abteilung für Transfusionsmedizin, Universitätsklinikum Tübingen, Universität Tübingen, D-72076 Tübingen, Germany. a-flieger@northwestern.edu
A
A
Flieger
S
S
Gong
M
M
Faigle
S
S
Stevanovic
N P
NP
Cianciotto
B
B
Neumeister
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D003470:Culture Media; D010450:Endopeptidases; D016952:Legionella pneumophila / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D008245:Lysophospholipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D003470:Culture Media; D008245:Lysophospholipase; D010450:Endopeptidases; C067127:prepilin peptidase protein, Bacteria