A family of eukaryotic lysophospholipid acyltransferases with broad specificity

FEBS Lett. 2008 Jan 23;582(2):305-9. doi: 10.1016/j.febslet.2007.12.020. Epub 2007 Dec 26.

Abstract

The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT (ScLPLAT) belongs to a distinct protein family that includes human MBOAT1, MBOAT2, MBOAT4, and several closely related proteins from other eukaryotes. We further show that two plant proteins within this family, the Arabidopsis proteins AtLPLAT1 and AtLPLAT2, possess lysophospholipid acyltransferase activities similar to ScLPLAT. We propose that other members of this protein family, which we refer to as the LPLAT family, also are likely to possess LPLAT activity. Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that it cannot efficiently use lysophosphatidic acid produced by acylation of glycerol-3-phosphate in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Acylglycerophosphocholine O-Acyltransferase / metabolism*
  • Animals
  • Base Sequence
  • DNA Primers
  • Humans
  • Phylogeny
  • Substrate Specificity

Substances

  • DNA Primers
  • 1-Acylglycerophosphocholine O-Acyltransferase