Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases
We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid Venturia canescens and its closest Drosophila relative, one of the putative PHGPx...
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| Veröffentlicht in: | Journal of insect physiology 2003, Vol.49 (1), p.1-9 |
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| container_title | Journal of insect physiology |
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| creator | Li, D. Blasevich, F. Theopold, U. Schmidt, O. |
| description | We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid
Venturia canescens and its closest
Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley
Drosophila genome sequence project. Recombinant
Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed. |
| doi_str_mv | 10.1016/S0022-1910(02)00189-0 |
| format | Article |
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Venturia canescens and its closest
Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley
Drosophila genome sequence project. Recombinant
Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed.</description><identifier>ISSN: 0022-1910</identifier><identifier>EISSN: 1879-1611</identifier><identifier>DOI: 10.1016/S0022-1910(02)00189-0</identifier><identifier>PMID: 12770011</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; DNA Primers ; Drosophila - classification ; Drosophila - enzymology ; Drosophila - genetics ; Drosophila - physiology ; Drosophila melanogaster ; Genome ; Glutathione Peroxidase - genetics ; Glutathione Peroxidase - metabolism ; Humans ; Hymenoptera - classification ; Hymenoptera - enzymology ; Hymenoptera - physiology ; Molecular Sequence Data ; Open Reading Frames ; Phospholipid hydroperoxide glutathione peroxidase ; Phylogeny ; Recombinant Proteins - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Substrate Specificity ; Transcription, Genetic ; Venturia canescens ; Virus-like particle-protein</subject><ispartof>Journal of insect physiology, 2003, Vol.49 (1), p.1-9</ispartof><rights>2002 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-10584e0690a3f801c104b796cc425ce825b0503f5c4308281f44bd538737ce193</citedby><cites>FETCH-LOGICAL-c458t-10584e0690a3f801c104b796cc425ce825b0503f5c4308281f44bd538737ce193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0022-1910(02)00189-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12770011$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, D.</creatorcontrib><creatorcontrib>Blasevich, F.</creatorcontrib><creatorcontrib>Theopold, U.</creatorcontrib><creatorcontrib>Schmidt, O.</creatorcontrib><title>Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases</title><title>Journal of insect physiology</title><addtitle>J Insect Physiol</addtitle><description>We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid
Venturia canescens and its closest
Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley
Drosophila genome sequence project. Recombinant
Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>DNA Primers</subject><subject>Drosophila - classification</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Drosophila - physiology</subject><subject>Drosophila melanogaster</subject><subject>Genome</subject><subject>Glutathione Peroxidase - genetics</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Humans</subject><subject>Hymenoptera - classification</subject><subject>Hymenoptera - enzymology</subject><subject>Hymenoptera - physiology</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Phospholipid hydroperoxide glutathione peroxidase</subject><subject>Phylogeny</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>Transcription, Genetic</subject><subject>Venturia canescens</subject><subject>Virus-like particle-protein</subject><issn>0022-1910</issn><issn>1879-1611</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQhq2qCJaPn9Aqp4oeAjN2nDgnVCFKK60EKnC2EmfSNcrGwU4K_Pt62QiOexiNNHreeaWHsS8IZwiYn98BcJ5iiXAK_DsAqjKFT2yBqihTzBE_s8U7csAOQ3gEAJkruc8OkBdFjOCC_bl1Idi6o6SdejNa1yeuTcZnl9g-kBmTYeVCnM4OtklXr413A3n3YhtK_nbTWI2rmKFkPlaBwjHba6su0Mm8j9jDz6v7y1_p8ub69-WPZWoyqcYUQaqMIC-hEq0CNAhZXZS5MRmXhhSXNUgQrTSZAMUVtllWN1KoQhSGsBRH7Nv27-Dd00Rh1GsbDHVd1ZObgi6E4DJ27ARR5UXOxeaj3ILGRyueWj14u678q0bQG-v6zbreKNXA9Zt1DTH3dS6Y6jU1H6lZcwQutgBFH_8seR2Mpd5QY32UrBtnd1T8Bz9XkVA</recordid><startdate>2003</startdate><enddate>2003</enddate><creator>Li, D.</creator><creator>Blasevich, F.</creator><creator>Theopold, U.</creator><creator>Schmidt, O.</creator><general>Elsevier 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>7SS</scope><scope>7X8</scope></search><sort><creationdate>2003</creationdate><title>Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases</title><author>Li, D. ; Blasevich, F. ; Theopold, U. ; Schmidt, O.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-10584e0690a3f801c104b796cc425ce825b0503f5c4308281f44bd538737ce193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>DNA Primers</topic><topic>Drosophila - classification</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - genetics</topic><topic>Drosophila - physiology</topic><topic>Drosophila melanogaster</topic><topic>Genome</topic><topic>Glutathione Peroxidase - genetics</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Humans</topic><topic>Hymenoptera - classification</topic><topic>Hymenoptera - enzymology</topic><topic>Hymenoptera - physiology</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames</topic><topic>Phospholipid hydroperoxide glutathione peroxidase</topic><topic>Phylogeny</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>Transcription, Genetic</topic><topic>Venturia canescens</topic><topic>Virus-like particle-protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, D.</creatorcontrib><creatorcontrib>Blasevich, F.</creatorcontrib><creatorcontrib>Theopold, U.</creatorcontrib><creatorcontrib>Schmidt, O.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of insect physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, D.</au><au>Blasevich, F.</au><au>Theopold, U.</au><au>Schmidt, O.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases</atitle><jtitle>Journal of insect physiology</jtitle><addtitle>J Insect Physiol</addtitle><date>2003</date><risdate>2003</risdate><volume>49</volume><issue>1</issue><spage>1</spage><epage>9</epage><pages>1-9</pages><issn>0022-1910</issn><eissn>1879-1611</eissn><abstract>We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid
Venturia canescens and its closest
Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley
Drosophila genome sequence project. Recombinant
Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>12770011</pmid><doi>10.1016/S0022-1910(02)00189-0</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of insect physiology, 2003, Vol.49 (1), p.1-9 |
| issn | 0022-1910 1879-1611 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence Animals Base Sequence Blotting, Northern DNA Primers Drosophila - classification Drosophila - enzymology Drosophila - genetics Drosophila - physiology Drosophila melanogaster Genome Glutathione Peroxidase - genetics Glutathione Peroxidase - metabolism Humans Hymenoptera - classification Hymenoptera - enzymology Hymenoptera - physiology Molecular Sequence Data Open Reading Frames Phospholipid hydroperoxide glutathione peroxidase Phylogeny Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Substrate Specificity Transcription, Genetic Venturia canescens Virus-like particle-protein |
| title | Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases |
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