Kinetic and structural characterization of triacylglycerol lipases possessing phospholipase A1 activity.
作者： Ahmed Aloulou , Fakher Frikha , Alexandre Noiriel , Madiha Bou Ali , Abdelkarim Abousalham
DOI: 10.1016/J.BBALIP.2013.12.009
关键词: Phospholipase A1 、 Lipoprotein lipase 、 Lipase 、 Phospholipase 、 Oxyanion hole 、 Biochemistry 、 Pancreatic lipase family 、 Phospholipase A 、 Monoacylglycerol lipase 、 Chemistry
摘要: The pancreatic lipase gene family displays various substrate selectivities for triglycerides and phospholipids. structural basis this difference in specificity has not been definitively established. Based on a kinetic comparative study between members, we showed here that porcine (PPL), which was so far classified as "classical lipase", able to hydrolyze phosphatidylcholine (PC). Amino acid sequence alignments revealed Val260 residue PPL lid could be critical the interaction with lipid substrate. Molecular dynamics applied investigate PC binding modes within catalytic cavity of human (HPL), aiming explain these enzymes towards Results HPL, oxyanion hole accommodate molecule, suggesting no activity obtained. With PPL, formation large pocket involving allowed molecule come near residues, it hydrolyzed. One more interesting finding is related protein 2 phospholipids through its PLA1 PLA2 activities. Overall, our shed light new features phospholipase members.
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