PAFAH2 hydrolyses PAF to lyso-PAF and acetate

Stable Identifier
Reaction [transition]
Homo sapiens
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Platelet-activating factor acetylhydrolase 2 (PAFAH2) (Rice et al. 1998) is an intracellular phospholipase A2 enzyme that inactivates the potent phospholipid mediator platelet-activating factor (PAF) and other structurally similar bioactive lipids produced in response to oxidative stress. PAFAH2 hydrolyses PAF at the sn-2 position, producing lyso-PAF and acetate (CH3COO-). Following oxidative stress, cytoplasmic PAFAH2 (present in homodimeric form) trafficks to the membranes of both the endoplasmic reticulum and Golgi apparatus; membrane localisation is critical for substrate acquisition and effective oxidative stress protection (Thevenin et al. 2011, Monillas et al. 2015). The enzyme that performs the last step in PAF synthesis is located on the outer leaf of the ER membrane. PAFAH2 ER localisation would allow it to access newly synthesized PAF, potentially serving as a control mechanism for PAF levels.
Literature References
PubMed ID Title Journal Year
21882811 Trafficking of platelet-activating factor acetylhydrolase type II in response to oxidative stress

Bahnson, BJ, Czymmek, K, Thévenin, AF, Winget, JM, Monillas, ES

Biochemistry 2011
25707358 Oligomeric state regulated trafficking of human platelet-activating factor acetylhydrolase type-II

Bahnson, BJ, Thévenin, AF, Caplan, JL, Monillas, ES

Biochim. Biophys. Acta 2015
9494101 Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor

Boyd, HF, Rice, SQ, MacPhee, CH, Tew, DG, Gloger, IS, Terrett, JA, Southan, C, Moores, K

Biochem. J. 1998
Catalyst Activity

1-alkyl-2-acetylglycerophosphocholine esterase activity of PAFAH2 [endoplasmic reticulum membrane]

Orthologous Events
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