Prokaryotic phospholipase A2

{{DISPLAYTITLE:Prokaryotic phospholipase A₂}}

{{Pfam_box

| Symbol = Phospholip_A2_3

| Name = Prokaryotic phospholipase A₂

| image = PDB 1kp4 EBI.jpg

| width =

| caption = Structure of prokaryotic phospholipase A₂.{{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 |doi-access=free }}

| 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.{{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|doi-access=free }}