Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes]
The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the β-oxidation pathway were determined: acyl-CoA oxidoreductase, enoyl-CoA hydr...
Gespeichert in:
| Veröffentlicht in: | Plant physiology (Bethesda) 1984-07, Vol.75 (3), p.531-533 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 533 |
|---|---|
| container_issue | 3 |
| container_start_page | 531 |
| container_title | Plant physiology (Bethesda) |
| container_volume | 75 |
| creator | Stabenau, H Winkler, U Saftel, W |
| description | The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the β-oxidation pathway were determined: acyl-CoA oxidoreductase, enoyl-CoA hydratase, and 3-hydroxyacyl-CoA dehydrogenase. There are indications that the peroxisomal oxidoreductase of both algae is a H2O2-forming oxidase rather than a dehydrogenase. The enzymes enoyl-CoA hydratase and acyl-CoA oxidoreductase are located also in the mitochondria from Eremosphaera but not from Mougeotia. The mitochondrial acyl-CoA oxidizing enzyme was found to be a dehydrogenase. The specific activities of acyl-CoA oxidase and enoyl-CoA hydratase are lower than in spinach leaf peroxisomes. However, the activity of 3-hydroxyacyl-CoA dehydrogenase in the peroxisomes of both algae is almost 2-fold higher. The capability for degradation of fatty acids is a common feature of all different types of peroxisomes from algae. |
| doi_str_mv | 10.1104/pp.75.3.531 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1066949</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>4268717</jstor_id><sourcerecordid>4268717</sourcerecordid><originalsourceid>FETCH-LOGICAL-c379t-1448544dba0bb0d512614c79abc00ddc548a36d43a8d42c7645038566a3aa28f3</originalsourceid><addsrcrecordid>eNpVkc1rFDEYxoModls9eRORHAQPdtZk8jGZiyBl_YCKB-1JJLyTZLYpM5OYzJauf70ps6x6Ssjz43nzvA9CzyhZU0r42xjXjViztWD0AVpRweqqFlw9RCtCyp0o1Z6g05xvCCGUUf4YnVApJZOSrNB-M_3ejy7j0OPOzVCFO29h9mHCfsLW971LbprxvI8LBMMWBjx6k0IXrC-PP76E3daF2QPOcX2ON8mNIcdrcAnwrU_e-nyOBwc9ji4V_xzKwJ9P0KMehuyeHs4zdPVh8_3iU3X59ePni_eXlWFNO1eUcyU4tx2QriNW0FpSbpoWOkOItaYkBSYtZ6Asr00juSBMCSmBAdSqZ2fo3eIbd93orClpEgw6Jj9C2usAXv-vTP5ab8OtpkTKlrfF4PXBIIVfO5dnPfps3DDA5MIu64Yx3hLa3JNvFrIsJ-fk-uMUSvR9VzpG3QjNdOmq0C___dhf9lBOAV4dAMgGhj7BZHw-ckqVzRBRsBcLdpPnkI4yr6VqaFPk54vcQ9CwTcXh6psSJR2p2R9qx7Ap</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733490179</pqid></control><display><type>article</type><title>Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes]</title><source>JSTOR Archive Collection A-Z Listing</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Stabenau, H ; Winkler, U ; Saftel, W</creator><creatorcontrib>Stabenau, H ; Winkler, U ; Saftel, W</creatorcontrib><description>The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the β-oxidation pathway were determined: acyl-CoA oxidoreductase, enoyl-CoA hydratase, and 3-hydroxyacyl-CoA dehydrogenase. There are indications that the peroxisomal oxidoreductase of both algae is a H2O2-forming oxidase rather than a dehydrogenase. The enzymes enoyl-CoA hydratase and acyl-CoA oxidoreductase are located also in the mitochondria from Eremosphaera but not from Mougeotia. The mitochondrial acyl-CoA oxidizing enzyme was found to be a dehydrogenase. The specific activities of acyl-CoA oxidase and enoyl-CoA hydratase are lower than in spinach leaf peroxisomes. However, the activity of 3-hydroxyacyl-CoA dehydrogenase in the peroxisomes of both algae is almost 2-fold higher. The capability for degradation of fatty acids is a common feature of all different types of peroxisomes from algae.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.75.3.531</identifier><identifier>PMID: 16663660</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Algae ; Biological and medical sciences ; Cell biochemistry ; Cell physiology ; Dehydrogenases ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Glycolates ; Glyoxysomes ; Microbodies ; Mitochondria ; Organelles ; Oxidases ; Peroxisomes ; Plant physiology and development</subject><ispartof>Plant physiology (Bethesda), 1984-07, Vol.75 (3), p.531-533</ispartof><rights>Copyright 1984 The American Society of Plant Physiologists</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-1448544dba0bb0d512614c79abc00ddc548a36d43a8d42c7645038566a3aa28f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4268717$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4268717$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27923,27924,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8848505$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16663660$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stabenau, H</creatorcontrib><creatorcontrib>Winkler, U</creatorcontrib><creatorcontrib>Saftel, W</creatorcontrib><title>Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes]</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the β-oxidation pathway were determined: acyl-CoA oxidoreductase, enoyl-CoA hydratase, and 3-hydroxyacyl-CoA dehydrogenase. There are indications that the peroxisomal oxidoreductase of both algae is a H2O2-forming oxidase rather than a dehydrogenase. The enzymes enoyl-CoA hydratase and acyl-CoA oxidoreductase are located also in the mitochondria from Eremosphaera but not from Mougeotia. The mitochondrial acyl-CoA oxidizing enzyme was found to be a dehydrogenase. The specific activities of acyl-CoA oxidase and enoyl-CoA hydratase are lower than in spinach leaf peroxisomes. However, the activity of 3-hydroxyacyl-CoA dehydrogenase in the peroxisomes of both algae is almost 2-fold higher. The capability for degradation of fatty acids is a common feature of all different types of peroxisomes from algae.</description><subject>Algae</subject><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>Dehydrogenases</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycolates</subject><subject>Glyoxysomes</subject><subject>Microbodies</subject><subject>Mitochondria</subject><subject>Organelles</subject><subject>Oxidases</subject><subject>Peroxisomes</subject><subject>Plant physiology and development</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNpVkc1rFDEYxoModls9eRORHAQPdtZk8jGZiyBl_YCKB-1JJLyTZLYpM5OYzJauf70ps6x6Ssjz43nzvA9CzyhZU0r42xjXjViztWD0AVpRweqqFlw9RCtCyp0o1Z6g05xvCCGUUf4YnVApJZOSrNB-M_3ejy7j0OPOzVCFO29h9mHCfsLW971LbprxvI8LBMMWBjx6k0IXrC-PP76E3daF2QPOcX2ON8mNIcdrcAnwrU_e-nyOBwc9ji4V_xzKwJ9P0KMehuyeHs4zdPVh8_3iU3X59ePni_eXlWFNO1eUcyU4tx2QriNW0FpSbpoWOkOItaYkBSYtZ6Asr00juSBMCSmBAdSqZ2fo3eIbd93orClpEgw6Jj9C2usAXv-vTP5ab8OtpkTKlrfF4PXBIIVfO5dnPfps3DDA5MIu64Yx3hLa3JNvFrIsJ-fk-uMUSvR9VzpG3QjNdOmq0C___dhf9lBOAV4dAMgGhj7BZHw-ckqVzRBRsBcLdpPnkI4yr6VqaFPk54vcQ9CwTcXh6psSJR2p2R9qx7Ap</recordid><startdate>19840701</startdate><enddate>19840701</enddate><creator>Stabenau, H</creator><creator>Winkler, U</creator><creator>Saftel, W</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19840701</creationdate><title>Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes]</title><author>Stabenau, H ; Winkler, U ; Saftel, W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-1448544dba0bb0d512614c79abc00ddc548a36d43a8d42c7645038566a3aa28f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Algae</topic><topic>Biological and medical sciences</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>Dehydrogenases</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycolates</topic><topic>Glyoxysomes</topic><topic>Microbodies</topic><topic>Mitochondria</topic><topic>Organelles</topic><topic>Oxidases</topic><topic>Peroxisomes</topic><topic>Plant physiology and development</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stabenau, H</creatorcontrib><creatorcontrib>Winkler, U</creatorcontrib><creatorcontrib>Saftel, W</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stabenau, H</au><au>Winkler, U</au><au>Saftel, W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes]</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1984-07-01</date><risdate>1984</risdate><volume>75</volume><issue>3</issue><spage>531</spage><epage>533</epage><pages>531-533</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the β-oxidation pathway were determined: acyl-CoA oxidoreductase, enoyl-CoA hydratase, and 3-hydroxyacyl-CoA dehydrogenase. There are indications that the peroxisomal oxidoreductase of both algae is a H2O2-forming oxidase rather than a dehydrogenase. The enzymes enoyl-CoA hydratase and acyl-CoA oxidoreductase are located also in the mitochondria from Eremosphaera but not from Mougeotia. The mitochondrial acyl-CoA oxidizing enzyme was found to be a dehydrogenase. The specific activities of acyl-CoA oxidase and enoyl-CoA hydratase are lower than in spinach leaf peroxisomes. However, the activity of 3-hydroxyacyl-CoA dehydrogenase in the peroxisomes of both algae is almost 2-fold higher. The capability for degradation of fatty acids is a common feature of all different types of peroxisomes from algae.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16663660</pmid><doi>10.1104/pp.75.3.531</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0032-0889 |
| ispartof | Plant physiology (Bethesda), 1984-07, Vol.75 (3), p.531-533 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1066949 |
| source | JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Algae Biological and medical sciences Cell biochemistry Cell physiology Dehydrogenases Enzymes Fundamental and applied biological sciences. Psychology Glycolates Glyoxysomes Microbodies Mitochondria Organelles Oxidases Peroxisomes Plant physiology and development |
| title | Enzymes of beta-oxidation in different types of algal microbodies [Mougeotia sp., Eremosphaera viridis, leaf peroxisomes] |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T13%3A33%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzymes%20of%20beta-oxidation%20in%20different%20types%20of%20algal%20microbodies%20%5BMougeotia%20sp.,%20Eremosphaera%20viridis,%20leaf%20peroxisomes%5D&rft.jtitle=Plant%20physiology%20(Bethesda)&rft.au=Stabenau,%20H&rft.date=1984-07-01&rft.volume=75&rft.issue=3&rft.spage=531&rft.epage=533&rft.pages=531-533&rft.issn=0032-0889&rft.eissn=1532-2548&rft.coden=PPHYA5&rft_id=info:doi/10.1104/pp.75.3.531&rft_dat=%3Cjstor_pubme%3E4268717%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=733490179&rft_id=info:pmid/16663660&rft_jstor_id=4268717&rfr_iscdi=true |