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SLC1 and SLC4 Encode Partially Redundant Acyl-Coenzyme A 1-Acylglycerol-3-phosphate O-Acyltransferases of Budding Yeast
Phosphatidic acid is the intermediate, from which all glycerophospholipids are synthesized. In yeast, it is generated from lysophosphatidic acid, which is acylated by Slc1p, an sn-2-specific, acyl-coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. Deletion of SLC1 is not lethal and d...
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| Published in: | The Journal of biological chemistry 2007-10, Vol.282 (42), p.30845-30855 |
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| container_issue | 42 |
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| creator | Benghezal, Mohammed Roubaty, Carole Veepuri, Vijayanath Knudsen, Jens Conzelmann, Andreas |
| description | Phosphatidic acid is the intermediate, from which all glycerophospholipids are synthesized. In yeast, it is generated from lysophosphatidic acid, which is acylated by Slc1p, an sn-2-specific, acyl-coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. Deletion of SLC1 is not lethal and does not eliminate all microsomal 1-acylglycerol-3-phosphate O-acyltransferase activity, suggesting that an additional enzyme may exist. Here we show that SLC4 (Yor175c), a gene of hitherto unknown function, encodes a second 1-acyl-sn-glycerol-3-phosphate acyltransferase. SLC4 harbors a membrane-bound O-acyltransferase motif and down-regulation of SLC4 strongly reduces 1-acyl-sn-glycerol-3-phosphate acyltransferase activity in microsomes from slc1Δ cells. The simultaneous deletion of SLC1 and SLC4 is lethal. Mass spectrometric analysis of lipids from slc1Δ and slc4Δ cells demonstrates that in vivo Slc1p and Slc4p generate almost the same glycerophospholipid profile. Microsomes from slc1Δ and slc4Δ cells incubated with [14C]oleoyl-coenzyme A in the absence of lysophosphatidic acid and without CTP still incorporate the label into glycerophospholipids, indicating that Slc1p and Slc4p can also use endogenous lysoglycerophospholipids as substrates. However, the lipid profiles generated by microsomes from slc1Δ and slc4Δ cells are different, and this suggests that Slc1p and Slc4p have a different substrate specificity or have access to different lyso-glycerophospholipid substrates because of a different subcellular location. Indeed, affinity-purified Slc1p displays Mg2+-dependent acyltransferase activity not only toward lysophosphatidic acid but also lyso forms of phosphatidylserine and phosphatidylinositol. Thus, Slc1p and Slc4p may not only be active as 1-acylglycerol-3-phosphate O-acyltransferases but also be involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids. |
| doi_str_mv | 10.1074/jbc.M702719200 |
| format | article |
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In yeast, it is generated from lysophosphatidic acid, which is acylated by Slc1p, an sn-2-specific, acyl-coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. Deletion of SLC1 is not lethal and does not eliminate all microsomal 1-acylglycerol-3-phosphate O-acyltransferase activity, suggesting that an additional enzyme may exist. Here we show that SLC4 (Yor175c), a gene of hitherto unknown function, encodes a second 1-acyl-sn-glycerol-3-phosphate acyltransferase. SLC4 harbors a membrane-bound O-acyltransferase motif and down-regulation of SLC4 strongly reduces 1-acyl-sn-glycerol-3-phosphate acyltransferase activity in microsomes from slc1Δ cells. The simultaneous deletion of SLC1 and SLC4 is lethal. Mass spectrometric analysis of lipids from slc1Δ and slc4Δ cells demonstrates that in vivo Slc1p and Slc4p generate almost the same glycerophospholipid profile. Microsomes from slc1Δ and slc4Δ cells incubated with [14C]oleoyl-coenzyme A in the absence of lysophosphatidic acid and without CTP still incorporate the label into glycerophospholipids, indicating that Slc1p and Slc4p can also use endogenous lysoglycerophospholipids as substrates. However, the lipid profiles generated by microsomes from slc1Δ and slc4Δ cells are different, and this suggests that Slc1p and Slc4p have a different substrate specificity or have access to different lyso-glycerophospholipid substrates because of a different subcellular location. Indeed, affinity-purified Slc1p displays Mg2+-dependent acyltransferase activity not only toward lysophosphatidic acid but also lyso forms of phosphatidylserine and phosphatidylinositol. Thus, Slc1p and Slc4p may not only be active as 1-acylglycerol-3-phosphate O-acyltransferases but also be involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M702719200</identifier><identifier>PMID: 17675291</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acyl Coenzyme A - chemistry ; Acyl Coenzyme A - genetics ; Acyl Coenzyme A - metabolism ; Acyltransferases - chemistry ; Acyltransferases - genetics ; Acyltransferases - metabolism ; Amino Acid Motifs - physiology ; Down-Regulation - physiology ; Dyneins ; Fatty Acids - chemistry ; Fatty Acids - genetics ; Fatty Acids - metabolism ; Gene Deletion ; Gene Expression Regulation, Enzymologic - physiology ; Glycerophospholipids - biosynthesis ; Glycerophospholipids - chemistry ; Glycerophospholipids - genetics ; Lipid Metabolism - physiology ; Lysophospholipids - metabolism ; Mass Spectrometry ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microsomes - enzymology ; Phosphotransferases (Alcohol Group Acceptor) - chemistry ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Substrate Specificity - physiology</subject><ispartof>The Journal of biological chemistry, 2007-10, Vol.282 (42), p.30845-30855</ispartof><rights>2007 © 2007 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-8ee41cb41af5ffa57bcb274fa0e29e5ad496ff052b77085953a4d54e0060d8a33</citedby><cites>FETCH-LOGICAL-c532t-8ee41cb41af5ffa57bcb274fa0e29e5ad496ff052b77085953a4d54e0060d8a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17675291$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Benghezal, Mohammed</creatorcontrib><creatorcontrib>Roubaty, Carole</creatorcontrib><creatorcontrib>Veepuri, Vijayanath</creatorcontrib><creatorcontrib>Knudsen, Jens</creatorcontrib><creatorcontrib>Conzelmann, Andreas</creatorcontrib><title>SLC1 and SLC4 Encode Partially Redundant Acyl-Coenzyme A 1-Acylglycerol-3-phosphate O-Acyltransferases of Budding Yeast</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Phosphatidic acid is the intermediate, from which all glycerophospholipids are synthesized. In yeast, it is generated from lysophosphatidic acid, which is acylated by Slc1p, an sn-2-specific, acyl-coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. Deletion of SLC1 is not lethal and does not eliminate all microsomal 1-acylglycerol-3-phosphate O-acyltransferase activity, suggesting that an additional enzyme may exist. Here we show that SLC4 (Yor175c), a gene of hitherto unknown function, encodes a second 1-acyl-sn-glycerol-3-phosphate acyltransferase. SLC4 harbors a membrane-bound O-acyltransferase motif and down-regulation of SLC4 strongly reduces 1-acyl-sn-glycerol-3-phosphate acyltransferase activity in microsomes from slc1Δ cells. The simultaneous deletion of SLC1 and SLC4 is lethal. Mass spectrometric analysis of lipids from slc1Δ and slc4Δ cells demonstrates that in vivo Slc1p and Slc4p generate almost the same glycerophospholipid profile. Microsomes from slc1Δ and slc4Δ cells incubated with [14C]oleoyl-coenzyme A in the absence of lysophosphatidic acid and without CTP still incorporate the label into glycerophospholipids, indicating that Slc1p and Slc4p can also use endogenous lysoglycerophospholipids as substrates. However, the lipid profiles generated by microsomes from slc1Δ and slc4Δ cells are different, and this suggests that Slc1p and Slc4p have a different substrate specificity or have access to different lyso-glycerophospholipid substrates because of a different subcellular location. Indeed, affinity-purified Slc1p displays Mg2+-dependent acyltransferase activity not only toward lysophosphatidic acid but also lyso forms of phosphatidylserine and phosphatidylinositol. Thus, Slc1p and Slc4p may not only be active as 1-acylglycerol-3-phosphate O-acyltransferases but also be involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids.</description><subject>Acyl Coenzyme A - chemistry</subject><subject>Acyl Coenzyme A - genetics</subject><subject>Acyl Coenzyme A - metabolism</subject><subject>Acyltransferases - chemistry</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Amino Acid Motifs - physiology</subject><subject>Down-Regulation - physiology</subject><subject>Dyneins</subject><subject>Fatty Acids - chemistry</subject><subject>Fatty Acids - genetics</subject><subject>Fatty Acids - metabolism</subject><subject>Gene Deletion</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Glycerophospholipids - biosynthesis</subject><subject>Glycerophospholipids - chemistry</subject><subject>Glycerophospholipids - genetics</subject><subject>Lipid Metabolism - physiology</subject><subject>Lysophospholipids - metabolism</subject><subject>Mass Spectrometry</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microsomes - enzymology</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - chemistry</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Substrate Specificity - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp1kE2P0zAQhiMEYsvClSP4gLiljB27To6lWj6kokUsK8HJcuxx41USFzthFX49Kam0J3wZa-aZV6Mny15SWFOQ_N1dbdZfJDBJKwbwKFtRKIu8EPTH42wFwGheMVFeZM9SuoP58Yo-zS6o3EjBKrrK7m_2O0p0b8n84eSqN8Ei-arj4HXbTuQb2rG3uh_I1kxtvgvY_5k6JFtC81Pn0E4GY2jzIj82IR0bPSC5_jcaou6Tw6gTJhIceT9a6_sD-Yk6Dc-zJ063CV-c62V2--Hq--5Tvr_--Hm33edGFGzIS0ROTc2pdsI5LWRtaia504CsQqEtrzbOgWC1lFCKShSaW8ERYAO21EVxmb1dco8x_BoxDarzyWDb6h7DmBSDAirKyxlcL6CJIaWITh2j73ScFAV1Uq1m1epB9bzw6pw81h3aB_zsdgbeLEDjD829j6hqH0yDnWIlU5ypAkouZuz1gjkdlD5En9TtDQNaAJRUAj0FlQuBs6jfHqNKxmNv0M6hZlA2-P8d-Rcvk6El</recordid><startdate>20071019</startdate><enddate>20071019</enddate><creator>Benghezal, Mohammed</creator><creator>Roubaty, Carole</creator><creator>Veepuri, Vijayanath</creator><creator>Knudsen, Jens</creator><creator>Conzelmann, Andreas</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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>M7N</scope></search><sort><creationdate>20071019</creationdate><title>SLC1 and SLC4 Encode Partially Redundant Acyl-Coenzyme A 1-Acylglycerol-3-phosphate O-Acyltransferases of Budding Yeast</title><author>Benghezal, Mohammed ; Roubaty, Carole ; Veepuri, Vijayanath ; Knudsen, Jens ; Conzelmann, Andreas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-8ee41cb41af5ffa57bcb274fa0e29e5ad496ff052b77085953a4d54e0060d8a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Acyl Coenzyme A - chemistry</topic><topic>Acyl Coenzyme A - genetics</topic><topic>Acyl Coenzyme A - metabolism</topic><topic>Acyltransferases - chemistry</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Amino Acid Motifs - physiology</topic><topic>Down-Regulation - physiology</topic><topic>Dyneins</topic><topic>Fatty Acids - chemistry</topic><topic>Fatty Acids - genetics</topic><topic>Fatty Acids - metabolism</topic><topic>Gene Deletion</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>Glycerophospholipids - biosynthesis</topic><topic>Glycerophospholipids - chemistry</topic><topic>Glycerophospholipids - genetics</topic><topic>Lipid Metabolism - physiology</topic><topic>Lysophospholipids - metabolism</topic><topic>Mass Spectrometry</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Microsomes - enzymology</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - chemistry</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Substrate Specificity - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Benghezal, Mohammed</creatorcontrib><creatorcontrib>Roubaty, Carole</creatorcontrib><creatorcontrib>Veepuri, Vijayanath</creatorcontrib><creatorcontrib>Knudsen, Jens</creatorcontrib><creatorcontrib>Conzelmann, Andreas</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Benghezal, Mohammed</au><au>Roubaty, Carole</au><au>Veepuri, Vijayanath</au><au>Knudsen, Jens</au><au>Conzelmann, Andreas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SLC1 and SLC4 Encode Partially Redundant Acyl-Coenzyme A 1-Acylglycerol-3-phosphate O-Acyltransferases of Budding Yeast</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2007-10-19</date><risdate>2007</risdate><volume>282</volume><issue>42</issue><spage>30845</spage><epage>30855</epage><pages>30845-30855</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>http://www.jbc.org/</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Phosphatidic acid is the intermediate, from which all glycerophospholipids are synthesized. In yeast, it is generated from lysophosphatidic acid, which is acylated by Slc1p, an sn-2-specific, acyl-coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. Deletion of SLC1 is not lethal and does not eliminate all microsomal 1-acylglycerol-3-phosphate O-acyltransferase activity, suggesting that an additional enzyme may exist. Here we show that SLC4 (Yor175c), a gene of hitherto unknown function, encodes a second 1-acyl-sn-glycerol-3-phosphate acyltransferase. SLC4 harbors a membrane-bound O-acyltransferase motif and down-regulation of SLC4 strongly reduces 1-acyl-sn-glycerol-3-phosphate acyltransferase activity in microsomes from slc1Δ cells. The simultaneous deletion of SLC1 and SLC4 is lethal. Mass spectrometric analysis of lipids from slc1Δ and slc4Δ cells demonstrates that in vivo Slc1p and Slc4p generate almost the same glycerophospholipid profile. Microsomes from slc1Δ and slc4Δ cells incubated with [14C]oleoyl-coenzyme A in the absence of lysophosphatidic acid and without CTP still incorporate the label into glycerophospholipids, indicating that Slc1p and Slc4p can also use endogenous lysoglycerophospholipids as substrates. However, the lipid profiles generated by microsomes from slc1Δ and slc4Δ cells are different, and this suggests that Slc1p and Slc4p have a different substrate specificity or have access to different lyso-glycerophospholipid substrates because of a different subcellular location. Indeed, affinity-purified Slc1p displays Mg2+-dependent acyltransferase activity not only toward lysophosphatidic acid but also lyso forms of phosphatidylserine and phosphatidylinositol. Thus, Slc1p and Slc4p may not only be active as 1-acylglycerol-3-phosphate O-acyltransferases but also be involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17675291</pmid><doi>10.1074/jbc.M702719200</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2007-10, Vol.282 (42), p.30845-30855 |
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| subjects | Acyl Coenzyme A - chemistry Acyl Coenzyme A - genetics Acyl Coenzyme A - metabolism Acyltransferases - chemistry Acyltransferases - genetics Acyltransferases - metabolism Amino Acid Motifs - physiology Down-Regulation - physiology Dyneins Fatty Acids - chemistry Fatty Acids - genetics Fatty Acids - metabolism Gene Deletion Gene Expression Regulation, Enzymologic - physiology Glycerophospholipids - biosynthesis Glycerophospholipids - chemistry Glycerophospholipids - genetics Lipid Metabolism - physiology Lysophospholipids - metabolism Mass Spectrometry Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Microsomes - enzymology Phosphotransferases (Alcohol Group Acceptor) - chemistry Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Substrate Specificity - physiology |
| title | SLC1 and SLC4 Encode Partially Redundant Acyl-Coenzyme A 1-Acylglycerol-3-phosphate O-Acyltransferases of Budding Yeast |
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