Catalytic residues of group VIB calcium-independent phospholipase A2 (iPLA2gamma)

Biochemical and Biophysical Research Communications
Haruki TanakaH Sumimoto

Abstract

Although human group VIB calcium-independent phospholipase A(2) (iPLA(2)gamma) contains the lipase-consensus sequence Gly-Xaa-Ser-Xaa-Gly in the C-terminal half, its overall sequence exhibits a week similarity to those of other PLA(2)s, and thus no information on the catalytic site has been available. Here we show that the C-terminal region of human iPLA(2)gamma is responsible for the enzymatic activity. Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad. Since substitution of alanine for either Ser-483 or Asp-627 results in a loss of the PLA(2) activity, we propose that Ser-483 and Asp-627 of human iPLA(2)gamma constitute an active site similar to the Ser-Asp dyad in cPLA(2) and patatin.

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Citations

Jun 25, 2013·Journal of Molecular Modeling·Gururao HariprasadReema Singh
Apr 28, 2006·Journal of Medicinal Chemistry·Daren StephensGeorge Kokotos
Dec 22, 2012·The Journal of Biological Chemistry·Hanan ElimamAndrey V Cybulsky
Sep 1, 2012·European Journal of Neurology : the Official Journal of the European Federation of Neurological Societies·P ZhangY Wu
May 30, 2015·Journal of Lipid Research·Sasanka RamanadhamXiaoyong Lei
Apr 13, 2011·Developmental Medicine and Child Neurology·Manju A KurianEamonn R Maher
Jan 5, 2005·Biochemical and Biophysical Research Communications·Gilbert R KinseyRick G Schnellmann

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