PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23701211-6	2013	Moreover, we demonstrate that the previously identified selective acylation of iPLA2beta by oleoyl-CoA occurs at C651 thereby indicating the importance of active site architecture for acylation of this enzyme.	oleoyl-coenzyme A	92-102	phospholipase A2 group VI	Homo sapiens	79-88	
23701211-7	2013	Collectively, these results identify C651 as a highly reactive nucleophilic residue within the active site of iPLA2beta which is thioesterified by BEL, acylated by oleoyl-CoA, and located in close spatial proximity to the catalytic serine thereby providing important chemical insights on the mechanisms through which BEL inhibits iPLA2beta and the topology of the active site.	oleoyl-coenzyme A	164-174	phospholipase A2 group VI	Homo sapiens	110-119