Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays)
Unlike animals which accumulate glutathione (gamma-glutamyl-L-cysteinyl-glycine) alone as their major thiol antioxidant, several crops synthesize alternative forms of glutathione by varying the carboxy residue. The molecular basis of this variation is not well understood, but the substrate specifici...
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Veröffentlicht in: | Biochemical journal 2005-11, Vol.391 (Pt 3), p.567-574 |
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description | Unlike animals which accumulate glutathione (gamma-glutamyl-L-cysteinyl-glycine) alone as their major thiol antioxidant, several crops synthesize alternative forms of glutathione by varying the carboxy residue. The molecular basis of this variation is not well understood, but the substrate specificity of the respective GSs (glutathione synthetases) has been implicated. To investigate their substrate tolerance, five GS-like cDNAs have been cloned from plants that can accumulate alternative forms of glutathione, notably soya bean [hGSH (homoglutathione or gamma-glutamyl-L-cysteinyl-beta-alanine)], wheat (hydroxymethylglutathione or gamma-glutamyl-L-cysteinyl-serine) and maize (gamma-Glu-Cys-Glu). The respective recombinant GSs were then assayed for the incorporation of differing C-termini into gamma-Glu-Cys. The soya bean enzyme primarily incorporated beta-alanine to form hGSH, whereas the GS enzymes from cereals preferentially catalysed the formation of glutathione. However, when assayed with other substrates, several GSs and one wheat enzyme in particular were able to synthesize a diverse range of glutathione variants by incorporating unusual C-terminal moieties including D-serine, non-natural amino acids and alpha-amino alcohols. Our results suggest that plant GSs are capable of producing a diverse range of glutathione homologues depending on the availability of the acyl acceptor. |
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The molecular basis of this variation is not well understood, but the substrate specificity of the respective GSs (glutathione synthetases) has been implicated. To investigate their substrate tolerance, five GS-like cDNAs have been cloned from plants that can accumulate alternative forms of glutathione, notably soya bean [hGSH (homoglutathione or gamma-glutamyl-L-cysteinyl-beta-alanine)], wheat (hydroxymethylglutathione or gamma-glutamyl-L-cysteinyl-serine) and maize (gamma-Glu-Cys-Glu). The respective recombinant GSs were then assayed for the incorporation of differing C-termini into gamma-Glu-Cys. The soya bean enzyme primarily incorporated beta-alanine to form hGSH, whereas the GS enzymes from cereals preferentially catalysed the formation of glutathione. However, when assayed with other substrates, several GSs and one wheat enzyme in particular were able to synthesize a diverse range of glutathione variants by incorporating unusual C-terminal moieties including D-serine, non-natural amino acids and alpha-amino alcohols. Our results suggest that plant GSs are capable of producing a diverse range of glutathione homologues depending on the availability of the acyl acceptor.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/BJ20050718</identifier><identifier>PMID: 16008521</identifier><language>eng</language><publisher>England: Portland Press Ltd</publisher><subject>Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Glutathione Synthase - genetics ; Glutathione Synthase - metabolism ; Glycine max - enzymology ; Glycine max - genetics ; Molecular Sequence Data ; Sequence Alignment ; Sequence Homology, Amino Acid ; Species Specificity ; Substrate Specificity ; Triticum - enzymology ; Triticum - genetics ; Zea mays - enzymology ; Zea mays - genetics</subject><ispartof>Biochemical journal, 2005-11, Vol.391 (Pt 3), p.567-574</ispartof><rights>The Biochemical Society, London 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-f9a9fb1d6b0f7708b2061da06d55e778b8c7b39c85457517822e16cad065c73b3</citedby><cites>FETCH-LOGICAL-c376t-f9a9fb1d6b0f7708b2061da06d55e778b8c7b39c85457517822e16cad065c73b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1276957/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1276957/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16008521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skipsey, Mark</creatorcontrib><creatorcontrib>Davis, Benjamin G</creatorcontrib><creatorcontrib>Edwards, Robert</creatorcontrib><title>Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays)</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Unlike animals which accumulate glutathione (gamma-glutamyl-L-cysteinyl-glycine) alone as their major thiol antioxidant, several crops synthesize alternative forms of glutathione by varying the carboxy residue. The molecular basis of this variation is not well understood, but the substrate specificity of the respective GSs (glutathione synthetases) has been implicated. To investigate their substrate tolerance, five GS-like cDNAs have been cloned from plants that can accumulate alternative forms of glutathione, notably soya bean [hGSH (homoglutathione or gamma-glutamyl-L-cysteinyl-beta-alanine)], wheat (hydroxymethylglutathione or gamma-glutamyl-L-cysteinyl-serine) and maize (gamma-Glu-Cys-Glu). The respective recombinant GSs were then assayed for the incorporation of differing C-termini into gamma-Glu-Cys. The soya bean enzyme primarily incorporated beta-alanine to form hGSH, whereas the GS enzymes from cereals preferentially catalysed the formation of glutathione. However, when assayed with other substrates, several GSs and one wheat enzyme in particular were able to synthesize a diverse range of glutathione variants by incorporating unusual C-terminal moieties including D-serine, non-natural amino acids and alpha-amino alcohols. Our results suggest that plant GSs are capable of producing a diverse range of glutathione homologues depending on the availability of the acyl acceptor.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>Gene Expression Regulation, Plant</subject><subject>Glutathione Synthase - genetics</subject><subject>Glutathione Synthase - metabolism</subject><subject>Glycine max - enzymology</subject><subject>Glycine max - genetics</subject><subject>Molecular Sequence Data</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>Substrate Specificity</subject><subject>Triticum - enzymology</subject><subject>Triticum - genetics</subject><subject>Zea mays - enzymology</subject><subject>Zea mays - genetics</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU9v1DAQxS0EokvhwgdAPqFdRGDsJLZzQYJSCqgSl3LhEo2dya5R_rSxs5B-BD41rrqi5TQjzU9v3tNj7LmANwIK-fbDVwlQghbmAVuJQkNmtDQP2QqkKjIFUhyxJyH8BBAFFPCYHQkFYEopVuzPR7-nKfjWO4x-HLgfeJhtiBNG4nPALXG78G03R4y7BBAPyxB3FDFQ4O009jyMC3JLOPD1Wbc4n5gef29e8187wsjXF5OP3s09RwrR7-d-w3FoEuOvia9_EKZ1CZun7FGLXaBnh3nMvn86vTj5nJ1_O_ty8v48c7lWMWsrrForGmWh1RqMlaBEg6CasiStjTVO27xypixKXQptpCShHDagSqdzmx-zd7e6l7PtqXE0pLBdfTn5HqelHtHX_18Gv6u3474WUquq1Eng5UFgGq_mlKnufXDUdTjQOIdamWRLV1UCX92CbhpDmKj990RAfVNdfVddgl_ct3WHHrrK_wIvOJYJ</recordid><startdate>20051101</startdate><enddate>20051101</enddate><creator>Skipsey, Mark</creator><creator>Davis, Benjamin G</creator><creator>Edwards, Robert</creator><general>Portland Press Ltd</general><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><scope>5PM</scope></search><sort><creationdate>20051101</creationdate><title>Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays)</title><author>Skipsey, Mark ; Davis, Benjamin G ; Edwards, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-f9a9fb1d6b0f7708b2061da06d55e778b8c7b39c85457517822e16cad065c73b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>Gene Expression Regulation, Plant</topic><topic>Glutathione Synthase - genetics</topic><topic>Glutathione Synthase - metabolism</topic><topic>Glycine max - enzymology</topic><topic>Glycine max - genetics</topic><topic>Molecular Sequence Data</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>Substrate Specificity</topic><topic>Triticum - enzymology</topic><topic>Triticum - genetics</topic><topic>Zea mays - enzymology</topic><topic>Zea mays - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skipsey, Mark</creatorcontrib><creatorcontrib>Davis, Benjamin G</creatorcontrib><creatorcontrib>Edwards, Robert</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skipsey, Mark</au><au>Davis, Benjamin G</au><au>Edwards, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays)</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2005-11-01</date><risdate>2005</risdate><volume>391</volume><issue>Pt 3</issue><spage>567</spage><epage>574</epage><pages>567-574</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Unlike animals which accumulate glutathione (gamma-glutamyl-L-cysteinyl-glycine) alone as their major thiol antioxidant, several crops synthesize alternative forms of glutathione by varying the carboxy residue. The molecular basis of this variation is not well understood, but the substrate specificity of the respective GSs (glutathione synthetases) has been implicated. To investigate their substrate tolerance, five GS-like cDNAs have been cloned from plants that can accumulate alternative forms of glutathione, notably soya bean [hGSH (homoglutathione or gamma-glutamyl-L-cysteinyl-beta-alanine)], wheat (hydroxymethylglutathione or gamma-glutamyl-L-cysteinyl-serine) and maize (gamma-Glu-Cys-Glu). The respective recombinant GSs were then assayed for the incorporation of differing C-termini into gamma-Glu-Cys. The soya bean enzyme primarily incorporated beta-alanine to form hGSH, whereas the GS enzymes from cereals preferentially catalysed the formation of glutathione. However, when assayed with other substrates, several GSs and one wheat enzyme in particular were able to synthesize a diverse range of glutathione variants by incorporating unusual C-terminal moieties including D-serine, non-natural amino acids and alpha-amino alcohols. Our results suggest that plant GSs are capable of producing a diverse range of glutathione homologues depending on the availability of the acyl acceptor.</abstract><cop>England</cop><pub>Portland Press Ltd</pub><pmid>16008521</pmid><doi>10.1042/BJ20050718</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Binding Sites Cloning, Molecular Gene Expression Regulation, Plant Glutathione Synthase - genetics Glutathione Synthase - metabolism Glycine max - enzymology Glycine max - genetics Molecular Sequence Data Sequence Alignment Sequence Homology, Amino Acid Species Specificity Substrate Specificity Triticum - enzymology Triticum - genetics Zea mays - enzymology Zea mays - genetics |
title | Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays) |
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