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...
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Published in: | Journal of bacteriology Vol. 183; no. 6; pp. 2121 - 2124 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
American Society for Microbiology
01-03-2001
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Series: | Note |
Subjects: | |
Online Access: | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Department of Microbiology-Immunology, Northwestern University Medical School, Searle 6-573, 320 E Superior St., Chicago, IL 60611. Phone: 001-312-503-1034. Fax: 001-312-503-1339. E-mail: a-flieger@northwestern.edu. Present address: Department of Microbiology and Immunology, Chandler Medical Center, University of Kentucky, Lexington, KY 40536. |
ISSN: | 0021-9193 1098-5530 |
DOI: | 10.1128/JB.183.6.2121-2124.2001 |