4fa0: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PAG16_HUMAN PAG16_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:19615464</ref> <ref>PMID:17374643</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
