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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

Published online by Cambridge University Press:  01 March 1999

PER-JOHAN JAKOBSSON
Affiliation:
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden
RALF MORGENSTERN
Affiliation:
Institute of Environmental Medicine, Karolinska Institutet, S-171 77 Stockholm, Sweden
JOSEPH MANCINI
Affiliation:
>Merck Frosst Centre For Therapeutic Research, Kirkland, Quebec H9H 3L1, Canada
ANTHONY FORD-HUTCHINSON
Affiliation:
>Merck Frosst Centre For Therapeutic Research, Kirkland, Quebec H9H 3L1, Canada
BENGT PERSSON
Affiliation:
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden
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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.

Type
FOR THE RECORD
Copyright
© 1999 The Protein Society

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