H. Alex Brown
Principle Investigator; Professor of Pharmacology, Chemistry, and Biochemistry; Associate Director, VICB;
Last active: 2/12/2015

Biochemical characterization of a Pseudomonas aeruginosa phospholipase D.

Spencer C, Brown HA
Biochemistry. 2015 54 (5): 1208-18

PMID: 25565226 · PMCID: PMC4337821 · DOI:10.1021/bi501291t

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.

MeSH Terms (8)

Bacterial Proteins Cell Line Humans Phospholipase D Pseudomonas aeruginosa Sequence Homology, Amino Acid Species Specificity Substrate Specificity

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