PE is hydrolyzed to 2-acyl LPE by PLA2G4C

Stable Identifier
R-HSA-1482892
Type
Reaction
Species
Homo sapiens
Compartment
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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.

Literature References
PubMed ID Title Journal Year
20705608 Interfacial kinetic and binding properties of mammalian group IVB phospholipase A2 (cPLA2beta) and comparison with the other cPLA2 isoforms

Lehr, M, Gelb, MH, Aloulou, A, Naika, GS, Bollinger, JG, Ghomashchi, F, Leslie, CC

J Biol Chem 2010
15944408 Roles of C-terminal processing, and involvement in transacylation reaction of human group IVC phospholipase A2 (cPLA2gamma)

Waku, K, Nakanishi, H, Yamashita, A, Kawagishi, N, Kamata, R, Sugiura, T, Suzuki, H

J Biochem 2005
19501189 Subcellular localization and lysophospholipase/transacylation activities of human group IVC phospholipase A2 (cPLA2gamma)

Waku, K, Tanaka, K, Kumazawa, T, Yamashita, A, Kamata, R, Sugiura, T, Koga, H, Suzuki, N

Biochim Biophys Acta 2009
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Participates
Catalyst Activity

phospholipase A1 activity of PLA2G4C [endoplasmic reticulum membrane]

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