Substrate Specificity of Soybean Lipoxidase
Purified soybean lipoxidase was used to test the substrate specificity of all cis , cis -methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer 50% as effective. The presence of calcium ions broadened the pattern of specificit...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1969-03, Vol.244 (5), p.1149-1151 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1151 |
|---|---|
| container_issue | 5 |
| container_start_page | 1149 |
| container_title | The Journal of biological chemistry |
| container_volume | 244 |
| creator | Holman, R T Egwim, P O Christie, W W |
| description | Purified soybean lipoxidase was used to test the substrate specificity of all cis , cis -methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer
50% as effective. The presence of calcium ions broadened the pattern of specificity. The rates of reaction of a series of
polyunsaturated acids in which chain length, number of double bonds, and positions of double bonds varied were tested with
crude lipoxidase in the presence of calcium ion. The substrates which exhibit high rates of reaction all possessed double
bonds at the 6th and 9th carbon atoms counting from the methyl group. Thus the terminal structure is critical to the specificity
of the enzyme. For enzyme reaction, the carboxyl group must not be sterically hindered, and the unsaturation at the 6th carbon
atom from the methyl end of the chain must be a double bond. |
| doi_str_mv | 10.1016/S0021-9258(18)91821-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76305447</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76305447</sourcerecordid><originalsourceid>FETCH-LOGICAL-c378t-c29e2a4f91abf57131d7df7fd865da8dd0ff16ef115dd07b38d39ded2feaa6793</originalsourceid><addsrcrecordid>eNo9kFtLxDAQhYMo67r6ExaKD6JINdM0TfIoizdY8KEKvoW0mbiR7bY2Lbr_3u6FnZeZ4ZwzAx8hU6B3QCG7zylNIFYJl9cgbxTIYYMjMgYqWcw4fB6T8cFySs5C-KZDpQpGZMQlJIqLMbnN-yJ0rekwyhssvfOl79ZR7aK8XhdoVtHcN_WftybgOTlxZhnwYt8n5OPp8X32Es_fnl9nD_O4ZEJ2cZkoTEzqFJjCcQEMrLBOOCszbo20ljoHGToAPsyiYNIyZdEmDo3JhGITcrW727T1T4-h05UPJS6XZoV1H7TIGOVpKgYj3xnLtg6hRaeb1lemXWugegNJbyHpDQENUm8haRhy0_2DvqjQHlJ7KoN-udMX_mvx61vUha_LBVY6SVPNNUCq2D-W724A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76305447</pqid></control><display><type>article</type><title>Substrate Specificity of Soybean Lipoxidase</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Holman, R T ; Egwim, P O ; Christie, W W</creator><creatorcontrib>Holman, R T ; Egwim, P O ; Christie, W W</creatorcontrib><description>Purified soybean lipoxidase was used to test the substrate specificity of all cis , cis -methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer
50% as effective. The presence of calcium ions broadened the pattern of specificity. The rates of reaction of a series of
polyunsaturated acids in which chain length, number of double bonds, and positions of double bonds varied were tested with
crude lipoxidase in the presence of calcium ion. The substrates which exhibit high rates of reaction all possessed double
bonds at the 6th and 9th carbon atoms counting from the methyl group. Thus the terminal structure is critical to the specificity
of the enzyme. For enzyme reaction, the carboxyl group must not be sterically hindered, and the unsaturation at the 6th carbon
atom from the methyl end of the chain must be a double bond.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)91821-1</identifier><identifier>PMID: 5812957</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Calcium ; Chemical Phenomena ; Chemistry ; Fatty Acids ; Glycine max ; Kinetics ; Linoleic Acids ; Lipids ; Oxygenases ; Seeds - enzymology</subject><ispartof>The Journal of biological chemistry, 1969-03, Vol.244 (5), p.1149-1151</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-c29e2a4f91abf57131d7df7fd865da8dd0ff16ef115dd07b38d39ded2feaa6793</citedby><cites>FETCH-LOGICAL-c378t-c29e2a4f91abf57131d7df7fd865da8dd0ff16ef115dd07b38d39ded2feaa6793</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5812957$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Holman, R T</creatorcontrib><creatorcontrib>Egwim, P O</creatorcontrib><creatorcontrib>Christie, W W</creatorcontrib><title>Substrate Specificity of Soybean Lipoxidase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Purified soybean lipoxidase was used to test the substrate specificity of all cis , cis -methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer
50% as effective. The presence of calcium ions broadened the pattern of specificity. The rates of reaction of a series of
polyunsaturated acids in which chain length, number of double bonds, and positions of double bonds varied were tested with
crude lipoxidase in the presence of calcium ion. The substrates which exhibit high rates of reaction all possessed double
bonds at the 6th and 9th carbon atoms counting from the methyl group. Thus the terminal structure is critical to the specificity
of the enzyme. For enzyme reaction, the carboxyl group must not be sterically hindered, and the unsaturation at the 6th carbon
atom from the methyl end of the chain must be a double bond.</description><subject>Calcium</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Fatty Acids</subject><subject>Glycine max</subject><subject>Kinetics</subject><subject>Linoleic Acids</subject><subject>Lipids</subject><subject>Oxygenases</subject><subject>Seeds - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtLxDAQhYMo67r6ExaKD6JINdM0TfIoizdY8KEKvoW0mbiR7bY2Lbr_3u6FnZeZ4ZwzAx8hU6B3QCG7zylNIFYJl9cgbxTIYYMjMgYqWcw4fB6T8cFySs5C-KZDpQpGZMQlJIqLMbnN-yJ0rekwyhssvfOl79ZR7aK8XhdoVtHcN_WftybgOTlxZhnwYt8n5OPp8X32Es_fnl9nD_O4ZEJ2cZkoTEzqFJjCcQEMrLBOOCszbo20ljoHGToAPsyiYNIyZdEmDo3JhGITcrW727T1T4-h05UPJS6XZoV1H7TIGOVpKgYj3xnLtg6hRaeb1lemXWugegNJbyHpDQENUm8haRhy0_2DvqjQHlJ7KoN-udMX_mvx61vUha_LBVY6SVPNNUCq2D-W724A</recordid><startdate>19690310</startdate><enddate>19690310</enddate><creator>Holman, R T</creator><creator>Egwim, P O</creator><creator>Christie, W W</creator><general>American Society for Biochemistry and Molecular Biology</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></search><sort><creationdate>19690310</creationdate><title>Substrate Specificity of Soybean Lipoxidase</title><author>Holman, R T ; Egwim, P O ; Christie, W W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-c29e2a4f91abf57131d7df7fd865da8dd0ff16ef115dd07b38d39ded2feaa6793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Calcium</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Fatty Acids</topic><topic>Glycine max</topic><topic>Kinetics</topic><topic>Linoleic Acids</topic><topic>Lipids</topic><topic>Oxygenases</topic><topic>Seeds - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Holman, R T</creatorcontrib><creatorcontrib>Egwim, P O</creatorcontrib><creatorcontrib>Christie, W W</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Holman, R T</au><au>Egwim, P O</au><au>Christie, W W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate Specificity of Soybean Lipoxidase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1969-03-10</date><risdate>1969</risdate><volume>244</volume><issue>5</issue><spage>1149</spage><epage>1151</epage><pages>1149-1151</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Purified soybean lipoxidase was used to test the substrate specificity of all cis , cis -methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer
50% as effective. The presence of calcium ions broadened the pattern of specificity. The rates of reaction of a series of
polyunsaturated acids in which chain length, number of double bonds, and positions of double bonds varied were tested with
crude lipoxidase in the presence of calcium ion. The substrates which exhibit high rates of reaction all possessed double
bonds at the 6th and 9th carbon atoms counting from the methyl group. Thus the terminal structure is critical to the specificity
of the enzyme. For enzyme reaction, the carboxyl group must not be sterically hindered, and the unsaturation at the 6th carbon
atom from the methyl end of the chain must be a double bond.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>5812957</pmid><doi>10.1016/S0021-9258(18)91821-1</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1969-03, Vol.244 (5), p.1149-1151 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76305447 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Calcium Chemical Phenomena Chemistry Fatty Acids Glycine max Kinetics Linoleic Acids Lipids Oxygenases Seeds - enzymology |
| title | Substrate Specificity of Soybean Lipoxidase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T05%3A34%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Substrate%20Specificity%20of%20Soybean%20Lipoxidase&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Holman,%20R%20T&rft.date=1969-03-10&rft.volume=244&rft.issue=5&rft.spage=1149&rft.epage=1151&rft.pages=1149-1151&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(18)91821-1&rft_dat=%3Cproquest_cross%3E76305447%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76305447&rft_id=info:pmid/5812957&rfr_iscdi=true |