Prokaryotic phospholipase A2

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Prokaryotic phospholipase A2
PDB 1kp4 EBI.jpg
Structure of prokaryotic phospholipase A2.[1]
Identifiers
Symbol Phospholip_A2_3
Pfam PF09056
InterPro IPR015141
OPM superfamily 90
OPM protein 1kp4

The prokaryotic phospholipase A2 domain is found in bacterial and fungal phospholipases. It enables the liberation of fatty acids and lysophospholipid by hydrolyzing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.[2]

References[edit]

  1. ^ Matoba Y, Katsube Y, Sugiyama M (May 2002). "The crystal structure of prokaryotic phospholipase A2". J. Biol. Chem. 277 (22): 20059–69. doi:10.1074/jbc.M200263200. PMID 11897785. 
  2. ^ Katsube Y, Sugiyama M, Matoba Y (2002). "The crystal structure of prokaryotic phospholipase A2". J. Biol. Chem. 277 (22): 20059–69. doi:10.1074/jbc.M200263200. PMID 11897785. 

This article incorporates text from the public domain Pfam and InterPro IPR015141