Distinctive structural features are shared by human, lapine, and murine acyloxyacyl hydrolases

Janet F. Staab, Susan Fosmire, Mei Zhang, Alan W. Varley, Robert S. Munford

Research output: Contribution to journalArticle

Abstract

Human acyloxyacyl hydrolase is an unusual lipase, found in phagocytic cells, that removes acyl chains from bacterial lipopolysaccharides (LPS) and glycerolipids. It is a heterodimer in which two glycosylated peptides are linked by disulfide bonding. The large subunit contains the active site serine, while the smaller subunit has striking sequence similarity to the saposins, peptide cofactors for several sphingolipid hydrolases. Since rabbits and mice are widely used for studies of LPS-animal interactions, we asked if murine and lapine AOAHs resemble the human enzyme. We report here that murine and lapine AOAHs share the distinctive features of the human AOAH primary sequence and have similar affinity for LPS. The structure of this unusual lipase appears to have been highly conserved.

Original languageEnglish (US)
Pages (from-to)205-208
Number of pages4
JournalInnate Immunity
Volume5
Issue number4
DOIs
StatePublished - Dec 1 1999

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ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Molecular Biology
  • Cell Biology
  • Infectious Diseases

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