Prokaryotic phospholipase A2
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| Prokaryotic phospholipase A2 | ||
|---|---|---|
| Identifiers | ||
| Symbol | Phospholip_A2_3 | |
| Pfam | PF09056 | |
| InterPro | IPR015141 | |
| OPM family | 90 | |
| OPM protein | 1kp4 | |
| Available PDB structures:
1lwbA:42-151 1it4A:42-151 1fazA:42-151 1kp4A:42-151 1it5A:42-149 |
||
The prokaryotic phospholipase A2 domain is found in bacterial and fungal phospholipases. It enables the liberation of fatty acids and lysophospholipid by hydrolysing 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 [1].
[edit] References
- ^ Katsube Y, Sugiyama M, Matoba Y (2002). "The crystal structure of prokaryotic phospholipase A2". J. Biol. Chem. 277 (22): -. PMID 11897785.
This article includes text from the public domain Pfam and InterPro IPR015141
