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Biochemistry. 2015 Feb 10;54(5):1208-18. doi: 10.1021/bi501291t. Epub 2015 Jan 22.

Biochemical characterization of a Pseudomonas aeruginosa phospholipase D.

Author information

1
Department of Pharmacology, ‡Department of Biochemistry, and Vanderbilt Institute of Chemical Biology, Vanderbilt University , Nashville, Tennessee 37232, United States.

Abstract

Phospholipase D is a ubiquitous protein in eukaryotes that hydrolyzes phospholipids to generate the signaling lipid phosphatidic acid (PtdOH). PldA, a Pseudomonas aeruginosa PLD, is a secreted protein that targets bacterial and eukaryotic cells. Here we have characterized the in vitro factors that modulate enzymatic activity of PldA, including divalent cations and phosphoinositides. We have identified several similarities between the eukaryotic-like PldA and the human PLD isoforms, as well as several properties in which the enzymes diverge. Notable differences include the substrate preference and transphosphatidylation efficiency for PldA. These findings offer new insights into potential regulatory mechanisms of PldA and its role in pathogenesis.

PMID:
25565226
PMCID:
PMC4337821
DOI:
10.1021/bi501291t
[Indexed for MEDLINE]
Free PMC Article

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