At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine (PE) is hydrolyzed, and has one of its acyl chains cleaved off by membrane-associated phospholipase A2 gamma 2A, PLA2G2A, to form 2-acyl lysophosphatidylethanolamine (LPE) (Yamashita et al. 2005, Ghomashchi et al. 2010, Yamashita et al. 2009). Cytosolic phospholipase A2 enzymes show not only PLA2 hydrolyzing activity to form the 1-acyl lysophospholipid but also have a degree of PLA1 activity, producing a 2-acyl lysophospholipid.
Lehr, M, Gelb, MH, Aloulou, A, Naika, GS, Bollinger, JG, Ghomashchi, F, Leslie, CC
Waku, K, Nakanishi, H, Yamashita, A, Kawagishi, N, Kamata, R, Sugiura, T, Suzuki, H
Waku, K, Tanaka, K, Kumazawa, T, Yamashita, A, Kamata, R, Sugiura, T, Koga, H, Suzuki, N
phospholipase A1 activity of PLA2G4C [endoplasmic reticulum membrane]
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