Prokaryotic phospholipase A2

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]

Prokaryotic phospholipase A2
Structure of prokaryotic phospholipase A2.[1]
Identifiers
SymbolPhospholip_A2_3
PfamPF09056
InterProIPR015141
OPM superfamily82
OPM protein1kp4

References

  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
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.