| 词条 | Prokaryotic phospholipase A2 |
| 释义 |
| Symbol = Phospholip_A2_3 | Name = Prokaryotic phospholipase A2 | image = PDB 1kp4 EBI.jpg | width = | caption = Structure of prokaryotic phospholipase A2.[1] | Pfam= PF09056 | InterPro= IPR015141 | SMART= | Prosite = | SCOP = | TCDB = | OPM family=82 | OPM protein= 1kp4 | PDB= }} 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] References1. ^{{cite journal |vauthors=Matoba Y, Katsube Y, Sugiyama M |title=The crystal structure of prokaryotic phospholipase A2 |journal=J. Biol. Chem. |volume=277 |issue=22 |pages=20059–69 |date=May 2002 |pmid=11897785 |doi=10.1074/jbc.M200263200 |url=}} {{InterPro content|IPR015141}}2. ^{{cite journal |vauthors=Katsube Y, Sugiyama M, Matoba Y |title=The crystal structure of prokaryotic phospholipase A2 |journal=J. Biol. Chem. |volume=277 |issue=22 |pages= 20059–69|year=2002 |pmid=11897785 |doi=10.1074/jbc.M200263200}} 2 : Protein domains|Peripheral membrane proteins |
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