NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803
Here we isolated and characterized two genes ( slr1171, slr1992) designated gpx-1 and gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from Synechocystis PCC 6803. The deduced amino acid sequences for gpx-1 and gpx-2 showed high similarity to those of GPX-like...
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| Veröffentlicht in: | FEBS letters 2001-06, Vol.499 (1), p.32-36 |
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| creator | Gaber, Ahmed Tamoi, Masahiro Takeda, Toru Nakano, Yoshihisa Shigeoka, Shigeru |
| description | Here we isolated and characterized two genes (
slr1171,
slr1992) designated
gpx-1 and
gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from
Synechocystis PCC 6803. The deduced amino acid sequences for
gpx-1 and
gpx-2 showed high similarity to those of GPX-like proteins from higher plants and mammalian GPXs, respectively. Surprisingly, both recombinant proteins in
Escherichia coli were able to utilize NADPH, but not reduced glutathione, as an electron donor and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides as an acceptor. It seems accurate to refer to Gpx-1 and Gpx-2 as NADPH-dependent GPX-like proteins that serve as a new defense system for the reduction of unsaturated fatty acid hydroperoxides. |
| doi_str_mv | 10.1016/S0014-5793(01)02517-0 |
| format | Article |
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slr1171,
slr1992) designated
gpx-1 and
gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from
Synechocystis PCC 6803. The deduced amino acid sequences for
gpx-1 and
gpx-2 showed high similarity to those of GPX-like proteins from higher plants and mammalian GPXs, respectively. Surprisingly, both recombinant proteins in
Escherichia coli were able to utilize NADPH, but not reduced glutathione, as an electron donor and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides as an acceptor. It seems accurate to refer to Gpx-1 and Gpx-2 as NADPH-dependent GPX-like proteins that serve as a new defense system for the reduction of unsaturated fatty acid hydroperoxides.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)02517-0</identifier><identifier>PMID: 11418106</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Cloning, Molecular ; Cyanobacteria - enzymology ; Cyanobacteria - genetics ; Cyanobacteria - metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Fatty Acids, Unsaturated - metabolism ; Glutathione Peroxidase - chemistry ; Glutathione Peroxidase - genetics ; Glutathione Peroxidase - isolation & purification ; Glutathione Peroxidase - metabolism ; Glutathione peroxidase-like protein ; GPX, glutathione peroxidase ; GSH, reduced glutathione ; Lipid Peroxides - metabolism ; Molecular Sequence Data ; Molecular Weight ; NADP - metabolism ; NADPH-dependent ; PHGPX, phospholipid hydroperoxide glutathione peroxidase ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sec, selenocysteine ; Sequence Alignment ; Substrate Specificity ; Synechocystis PCC 6803 ; Unsaturated fatty acid hydroperoxide</subject><ispartof>FEBS letters, 2001-06, Vol.499 (1), p.32-36</ispartof><rights>2001 Federation of European Biochemical Societies</rights><rights>FEBS Letters 499 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4920-9c3e239415e513b2cc1cddd5f6a1227dc6a7b9dd08ca8f06faf6460097111bc23</citedby><cites>FETCH-LOGICAL-c4920-9c3e239415e513b2cc1cddd5f6a1227dc6a7b9dd08ca8f06faf6460097111bc23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2801%2902517-0$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579301025170$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11418106$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gaber, Ahmed</creatorcontrib><creatorcontrib>Tamoi, Masahiro</creatorcontrib><creatorcontrib>Takeda, Toru</creatorcontrib><creatorcontrib>Nakano, Yoshihisa</creatorcontrib><creatorcontrib>Shigeoka, Shigeru</creatorcontrib><title>NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Here we isolated and characterized two genes (
slr1171,
slr1992) designated
gpx-1 and
gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from
Synechocystis PCC 6803. The deduced amino acid sequences for
gpx-1 and
gpx-2 showed high similarity to those of GPX-like proteins from higher plants and mammalian GPXs, respectively. Surprisingly, both recombinant proteins in
Escherichia coli were able to utilize NADPH, but not reduced glutathione, as an electron donor and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides as an acceptor. It seems accurate to refer to Gpx-1 and Gpx-2 as NADPH-dependent GPX-like proteins that serve as a new defense system for the reduction of unsaturated fatty acid hydroperoxides.</description><subject>Amino Acid Sequence</subject><subject>Cloning, Molecular</subject><subject>Cyanobacteria - enzymology</subject><subject>Cyanobacteria - genetics</subject><subject>Cyanobacteria - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Fatty Acids, Unsaturated - metabolism</subject><subject>Glutathione Peroxidase - chemistry</subject><subject>Glutathione Peroxidase - genetics</subject><subject>Glutathione Peroxidase - isolation & purification</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Glutathione peroxidase-like protein</subject><subject>GPX, glutathione peroxidase</subject><subject>GSH, reduced glutathione</subject><subject>Lipid Peroxides - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>NADP - metabolism</subject><subject>NADPH-dependent</subject><subject>PHGPX, phospholipid hydroperoxide glutathione peroxidase</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sec, selenocysteine</subject><subject>Sequence Alignment</subject><subject>Substrate Specificity</subject><subject>Synechocystis PCC 6803</subject><subject>Unsaturated fatty acid hydroperoxide</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUU1v1DAQtRAV3RZ-Asgn1EoEZpzESU5V2X4sUgWVCmfLa09YQzZZbKdt_gK_usnuCo5wmhnPmzee9xh7jfAeAeWHOwDMkryo0hPAUxA5Fgk8YzMsizRJM1k-Z7M_kEN2FMIPGOsSqxfsEDEbM5Az9vvz-cXtIrG0odZSG_n3po86rlzXEt-Q7x6d1YGSxv0ca99Fcm3gJ9ebxwTf8SmIU-7J9oZ43wYde68jWV7rGAeujbN8NVjf7akocNfyu6Els-rMEKIL_HY-57KE9CU7qHUT6NU-HrNvV5df54vk5sv1p_n5TWKySkBSmZREWmWYU47pUhiDxlqb11KjEIU1UhfLyloojS5rkLWuZSYBqgIRl0akx-ztjnc851dPIaq1C4aaRrfU9UEVUMlcimoE5jug8V0Inmq18W6t_aAQ1GSC2pqgJoUVoNqaoGCce7Nf0C_XZP9O7VUfAYsd4ME1NPwfq7q6_Ci2nakBuH2edp3tqGhU7N6RV8E4ag1Z58lEZTv3j98-AZ7sqts</recordid><startdate>20010615</startdate><enddate>20010615</enddate><creator>Gaber, Ahmed</creator><creator>Tamoi, Masahiro</creator><creator>Takeda, Toru</creator><creator>Nakano, Yoshihisa</creator><creator>Shigeoka, Shigeru</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20010615</creationdate><title>NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803</title><author>Gaber, Ahmed ; Tamoi, Masahiro ; Takeda, Toru ; Nakano, Yoshihisa ; Shigeoka, Shigeru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4920-9c3e239415e513b2cc1cddd5f6a1227dc6a7b9dd08ca8f06faf6460097111bc23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Cloning, Molecular</topic><topic>Cyanobacteria - enzymology</topic><topic>Cyanobacteria - genetics</topic><topic>Cyanobacteria - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Fatty Acids, Unsaturated - metabolism</topic><topic>Glutathione Peroxidase - chemistry</topic><topic>Glutathione Peroxidase - genetics</topic><topic>Glutathione Peroxidase - isolation & purification</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Glutathione peroxidase-like protein</topic><topic>GPX, glutathione peroxidase</topic><topic>GSH, reduced glutathione</topic><topic>Lipid Peroxides - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>NADP - metabolism</topic><topic>NADPH-dependent</topic><topic>PHGPX, phospholipid hydroperoxide glutathione peroxidase</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sec, selenocysteine</topic><topic>Sequence Alignment</topic><topic>Substrate Specificity</topic><topic>Synechocystis PCC 6803</topic><topic>Unsaturated fatty acid hydroperoxide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gaber, Ahmed</creatorcontrib><creatorcontrib>Tamoi, Masahiro</creatorcontrib><creatorcontrib>Takeda, Toru</creatorcontrib><creatorcontrib>Nakano, Yoshihisa</creatorcontrib><creatorcontrib>Shigeoka, Shigeru</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gaber, Ahmed</au><au>Tamoi, Masahiro</au><au>Takeda, Toru</au><au>Nakano, Yoshihisa</au><au>Shigeoka, Shigeru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-06-15</date><risdate>2001</risdate><volume>499</volume><issue>1</issue><spage>32</spage><epage>36</epage><pages>32-36</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Here we isolated and characterized two genes (
slr1171,
slr1992) designated
gpx-1 and
gpx-2, respectively, encoding glutathione peroxidase (GPX)-like proteins (Gpx-1, Gpx-2) from
Synechocystis PCC 6803. The deduced amino acid sequences for
gpx-1 and
gpx-2 showed high similarity to those of GPX-like proteins from higher plants and mammalian GPXs, respectively. Surprisingly, both recombinant proteins in
Escherichia coli were able to utilize NADPH, but not reduced glutathione, as an electron donor and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides as an acceptor. It seems accurate to refer to Gpx-1 and Gpx-2 as NADPH-dependent GPX-like proteins that serve as a new defense system for the reduction of unsaturated fatty acid hydroperoxides.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11418106</pmid><doi>10.1016/S0014-5793(01)02517-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2001-06, Vol.499 (1), p.32-36 |
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| subjects | Amino Acid Sequence Cloning, Molecular Cyanobacteria - enzymology Cyanobacteria - genetics Cyanobacteria - metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Fatty Acids, Unsaturated - metabolism Glutathione Peroxidase - chemistry Glutathione Peroxidase - genetics Glutathione Peroxidase - isolation & purification Glutathione Peroxidase - metabolism Glutathione peroxidase-like protein GPX, glutathione peroxidase GSH, reduced glutathione Lipid Peroxides - metabolism Molecular Sequence Data Molecular Weight NADP - metabolism NADPH-dependent PHGPX, phospholipid hydroperoxide glutathione peroxidase Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sec, selenocysteine Sequence Alignment Substrate Specificity Synechocystis PCC 6803 Unsaturated fatty acid hydroperoxide |
| title | NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803 |
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