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Novel lysophospholipase A secreted by Legionella pneumophila.


ABSTRACT: 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.

SUBMITTER: Flieger A 

PROVIDER: S-EPMC95111 | biostudies-literature | 2001 Mar

REPOSITORIES: biostudies-literature

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Novel lysophospholipase A secreted by Legionella pneumophila.

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]

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