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Common structural features of MAPEG— A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism

  • PER-JOHAN JAKOBSSON (a1), RALF MORGENSTERN (a2), JOSEPH MANCINI (a3), ANTHONY FORD-HUTCHINSON (a3) and BENGT PERSSON (a1)...
    • Published online by Cambridge University Press: 01 March 1999

Abstract

A novel superfamily designated MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism), including members of widespread origin with diversified biological functions is defined according to enzymatic activities, sequence motifs, and structural properties. Two of the members are crucial for leukotriene biosynthesis, and three are cytoprotective exhibiting glutathione S-transferase and peroxidase activities. Expression of the most recently recognized member is strongly induced by p53, and may therefore play a role in apoptosis or cancer development. In spite of the different biological functions, all six proteins demonstrate common structural characteristics typical of membrane proteins. In addition, homologues are identified in plants, fungi, and bacteria, demonstrating this superfamily to be generally occurring.

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Corresponding author

Reprint requests to: Per-Johan Jakobsson, Department of Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, S-171 77 Stockholm, Sweden; e-mail: per-johan.jakobsson@mbb.ki.se.
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Protein Science
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  • URL: /core/journals/protein-science
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