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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Culture Media
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Endopeptidases*
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Legionella pneumophila / enzymology*
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Legionella pneumophila / genetics
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Legionella pneumophila / growth & development
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Lysophospholipase / chemistry
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Lysophospholipase / genetics
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Lysophospholipase / metabolism*
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Molecular Sequence Data
Substances
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Bacterial Proteins
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Culture Media
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Lysophospholipase
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Endopeptidases
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prepilin peptidase protein, Bacteria