phospholipase D activity

Definition

Target type: molecularfunction

Catalysis of the reaction: a phosphatidylcholine + H2O = choline + a phosphatidate. [EC:3.1.4.4]

Phospholipase D (PLD) activity is a crucial enzymatic function involved in the hydrolysis of phospholipids, specifically phosphatidylcholine (PC), into phosphatidic acid (PA) and a headgroup, typically choline. This reaction plays a pivotal role in various cellular processes, including signal transduction, membrane trafficking, and cytoskeletal organization. PLD enzymes catalyze the cleavage of the phosphodiester bond linking the diacylglycerol moiety of PC to its choline headgroup. This hydrolysis reaction occurs at the sn-3 position of the glycerol backbone of PC, generating PA as a key signaling molecule. PA is a potent second messenger that can activate downstream signaling pathways, including the protein kinase C (PKC) pathway. Additionally, PA can interact with other signaling molecules and proteins, modulating membrane fluidity and influencing the dynamics of membrane trafficking events. Notably, PLD activity is tightly regulated by various factors, including calcium ions, GTPases, and phosphoinositide signaling. This intricate regulation allows for the precise control of PA production and the fine-tuning of cellular responses in different physiological contexts. Furthermore, PLD activity has been implicated in diverse pathological conditions, including cancer, inflammation, and neurological disorders. Understanding the molecular functions of PLD enzymes is essential for unraveling their roles in health and disease, paving the way for potential therapeutic interventions targeting PLD activity.'
"

Proteins (6)

Compounds (14)