Summary: | Secretory group V phospholipase A2 (PLA<sub>2</sub>-V) is known to be involved in inflammatory processes in cellular studies, nevertheless, the biochemical and the enzymatic characteristics of this important enzyme have been unclear yet. We reported, as a first step towards understanding the biochemical properties, catalytic characteristics, antimicrobial and cytotoxic effects of this PLA<sub>2</sub>, the production of PLA<sub>2</sub>-V from dromedary. The obtained DrPLA<sub>2</sub>-V has an absolute requirement for Ca<sup>2+</sup> and NaTDC for enzymatic activity with an optimum pH of 9 and temperature of 45 °C with phosphatidylethanolamine as a substrate. Kinetic parameters showed that <i>K<sub>cat</sub></i>/<i>Km</i><sub>app</sub> is 2.6 ± 0.02 mM<sup>−1</sup> s<sup>−1</sup>. The enzyme was found to display potent Gram-positive bactericidal activity (with IC50 values of about 5 µg/mL) and antifungal activity (with IC50 values of about 25 µg/mL)in vitro. However, the purified enzyme did not display a cytotoxic effect against cancer cells.
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