KNOWPIA
WELCOME TO KNOWPIA
Prokaryotic phospholipase A2 
Summary
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 | |||||||||
| Symbol | Phospholip_A2_3 | ||||||||
| Pfam | PF09056 | ||||||||
| InterPro | IPR015141 | ||||||||
| OPM superfamily | 82 | ||||||||
| OPM protein | 1kp4 | ||||||||
| |||||||||
References edit
- ^ 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.
- ^ 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.