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Bioinformatic and e...
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Bresell, AndersLinköpings universitet,Bioinformatik,Tekniska högskolan
(author)
Bioinformatic and enzymatic characterization of the MAPEG superfamily
- Article/chapterEnglish2005
Publisher, publication year, extent ...
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2005-03-09
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Wiley,2005
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:liu-12886
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https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-12886URI
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https://doi.org/10.1111/j.1742-4658.2005.04596.xDOI
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http://kipublications.ki.se/Default.aspx?queryparsed=id:110978124URI
Supplementary language notes
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Language:English
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Summary in:English
Part of subdatabase
Classification
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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The membrane associated proteins in eicosanoid and glutathione metabolism (MAPEG) superfamily includes structurally related membrane proteins with diverse functions of widespread origin. A total of 136 proteins belonging to the MAPEG superfamily were found in database and genome screenings. The members were found in prokaryotes and eukaryotes, but not in any archaeal organism. Multiple sequence alignments and calculations of evolutionary trees revealed a clear subdivision of the eukaryotic MAPEG members, corresponding to the six families of microsomal glutathione transferases (MGST) 1, 2 and 3, leukotriene C4 synthase (LTC4), 5-lipoxygenase activating protein (FLAP), and prostaglandin E synthase. Prokaryotes contain at least two distinct potential ancestral subfamilies, of which one is unique, whereas the other most closely resembles enzymes that belong to the MGST2/FLAP/LTC4 synthase families. The insect members are most similar to MGST1/prostaglandin E synthase. With the new data available, we observe that fish enzymes are present in all six families, showing an early origin for MAPEG family differentiation. Thus, the evolutionary origins and relationships of the MAPEG superfamily can be defined, including distinct sequence patterns characteristic for each of the subfamilies. We have further investigated and functionally characterized representative gene products from Escherichia coli, Synechocystis sp., Arabidopsis thaliana and Drosophila melanogaster, and the fish liver enzyme, purified from pike (Esox lucius). Protein overexpression and enzyme activity analysis demonstrated that all proteins catalyzed the conjugation of 1-chloro-2,4-dinitrobenzene with reduced glutathione. The E. coli protein displayed glutathione transferase activity of 0.11 µmol·min−1·mg−1 in the membrane fraction from bacteria overexpressing the protein. Partial purification of the Synechocystis sp. protein yielded an enzyme of the expected molecular mass and an N-terminal amino acid sequence that was at least 50% pure, with a specific activity towards 1-chloro-2,4-dinitrobenzene of 11 µmol·min−1·mg−1. Yeast microsomes expressing the Arabidopsis enzyme showed an activity of 0.02 µmol·min−1·mg−1, whereas the Drosophila enzyme expressed in E. coli was highly active at 3.6 µmol·min−1·mg−1. The purified pike enzyme is the most active MGST described so far with a specific activity of 285 µmol·min−1·mg−1. Drosophila and pike enzymes also displayed glutathione peroxidase activity towards cumene hydroperoxide (0.4 and 2.2 µmol·min−1·mg−1, respectively). Glutathione transferase activity can thus be regarded as a common denominator for a majority of MAPEG members throughout the kingdoms of life whereas glutathione peroxidase activity occurs in representatives from the MGST1, 2 and 3 and PGES subfamilies.
Subject headings and genre
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MAPEG
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microsomal glutathione transferase
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prostaglandin
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leukotriene
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NATURAL SCIENCES
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NATURVETENSKAP
Added entries (persons, corporate bodies, meetings, titles ...)
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Weinander, RolfDepartment of Medicine, Division of Rheumatology Unit, Karolinska Institutet, Stockholm
(author)
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Wiklund, RonneyDepartment of Plant Biology & Forestry Genetics, Swedish Agricultural University, Uppsala
(author)
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Eriksson, JanDepartment of Plant Biology & Forestry Genetics, Swedish Agricultural University, Uppsala
(author)
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Jansson, ChristerDepartment of Plant Biology & Forestry Genetics, Swedish Agricultural University, Uppsala
(author)
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Persson, BengtKarolinska Institutet,Linköpings universitet,Bioinformatik,Tekniska högskolan(Swepub:liu)benpe05
(author)
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Jakobsson, Per-JohanKarolinska Institutet
(author)
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Morgenstern, RalfKarolinska Institutet
(author)
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Lundqvist, GerdInstitute of Environmental Medicine Karolinska Institutet, Stockholm
(author)
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Raza, HaiderInstitute of Environmental Medicine Karolinska Institutet, Stockholm
(author)
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Shimoji, MiyukiInstitute of Environmental Medicine Karolinska Institutet, Stockholm
(author)
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Sun, Tie-HuaInstitute of Environmental Medicine Karolinska Institutet, Stockholm
(author)
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Balk, LennartStockholm Marine Research Centre, University of Stockholm
(author)
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Linköpings universitetBioinformatik
(creator_code:org_t)
Related titles
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In:The FEBS Journal: Wiley272:7, s. 1688-17031742-464X1742-4658
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