Catalytic residues of group VIB calcium-independent phospholipase A 2 (iPLA2γ)

Haruki Tanaka, Reiko Minakami, Hideki Kanaya, Hideki Sumimoto

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Although human group VIB calcium-independent phospholipase A2 (iPLA2γ) 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 PLA2s, and thus no information on the catalytic site has been available. Here we show that the C-terminal region of human iPLA2γ is responsible for the enzymatic activity. Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA2 (cPLA2), and the plant PLA2 patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA2γ is conserved among these PLA2s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA2 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 PLA2 activity, we propose that Ser-483 and Asp-627 of human iPLA 2γ constitute an active site similar to the Ser-Asp dyad in cPLA2 and patatin.

Original languageEnglish
Pages (from-to)1284-1290
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume320
Issue number4
DOIs
Publication statusPublished - Aug 6 2004

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Calcium-Independent Phospholipase A2
Phospholipases A
Lipase
Calcium
Catalytic Domain
Aspartic Acid
Alanine
Serine
Substitution reactions
Amino Acids
Consensus Sequence
Amino Acid Sequence

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Catalytic residues of group VIB calcium-independent phospholipase A 2 (iPLA2γ). / Tanaka, Haruki; Minakami, Reiko; Kanaya, Hideki; Sumimoto, Hideki.

In: Biochemical and Biophysical Research Communications, Vol. 320, No. 4, 06.08.2004, p. 1284-1290.

Research output: Contribution to journalArticle

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N2 - Although human group VIB calcium-independent phospholipase A2 (iPLA2γ) 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 PLA2s, and thus no information on the catalytic site has been available. Here we show that the C-terminal region of human iPLA2γ is responsible for the enzymatic activity. Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA2 (cPLA2), and the plant PLA2 patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA2γ is conserved among these PLA2s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA2 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 PLA2 activity, we propose that Ser-483 and Asp-627 of human iPLA 2γ constitute an active site similar to the Ser-Asp dyad in cPLA2 and patatin.

AB - Although human group VIB calcium-independent phospholipase A2 (iPLA2γ) 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 PLA2s, and thus no information on the catalytic site has been available. Here we show that the C-terminal region of human iPLA2γ is responsible for the enzymatic activity. Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA2 (cPLA2), and the plant PLA2 patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA2γ is conserved among these PLA2s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA2 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 PLA2 activity, we propose that Ser-483 and Asp-627 of human iPLA 2γ constitute an active site similar to the Ser-Asp dyad in cPLA2 and patatin.

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