Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli
Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 1979-03, Vol.203 (4385), p.1111-1112 |
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creator | Garnak, Margit Reeves, Henry C. |
description | Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified. |
doi_str_mv | 10.1126/science.34215 |
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This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.34215</identifier><identifier>PMID: 34215</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Acetates ; Acetates - metabolism ; Bacteria ; Citrates ; Dehydrogenases ; Enzymes ; Escherichia coli - enzymology ; Gels ; Isocitrate Dehydrogenase - metabolism ; Isocitrates ; NADP - metabolism ; Phosphorylation ; Protein Kinases - metabolism ; Radioactive decay ; Serine - metabolism ; Sodium ; Threonine - metabolism</subject><ispartof>Science (American Association for the Advancement of Science), 1979-03, Vol.203 (4385), p.1111-1112</ispartof><rights>Copyright 1979 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c307t-844a6a74928b8e435ad9c976aa17f4344b6da3221d469d18f972f06628359ae33</citedby><cites>FETCH-LOGICAL-c307t-844a6a74928b8e435ad9c976aa17f4344b6da3221d469d18f972f06628359ae33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/1747387$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/1747387$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Garnak, Margit</creatorcontrib><creatorcontrib>Reeves, Henry C.</creatorcontrib><title>Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified.</description><subject>Acetates</subject><subject>Acetates - metabolism</subject><subject>Bacteria</subject><subject>Citrates</subject><subject>Dehydrogenases</subject><subject>Enzymes</subject><subject>Escherichia coli - enzymology</subject><subject>Gels</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Isocitrates</subject><subject>NADP - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Radioactive decay</subject><subject>Serine - metabolism</subject><subject>Sodium</subject><subject>Threonine - metabolism</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkL1OwzAYRS1EBaEwMsGQF0ix_Tn-mRAqBSpVggHm6KvjEFdtXdlhyNv3F5jucI6udC8ht4yOGOPyIVnv1taNQHBWnpGMUVMWhlM4JxmlIAtNVXlJrlJaULpjBi7I4CBn5PGjDWnThtgvsfNhnYcmn6ZgfRexc_mza_s6hm-3xuT2bJJs66K3rcfchqW_JoMGl8ndnHJIvl4mn-O3Yvb-Oh0_zQoLVHWFFgIlKmG4nmsnoMTaWKMkIlONACHmskbgnNVCmprpxijeUCm5htKgAxiS4thrY0gpuqbaRL_C2FeMVvsXqtML1WHYzr87-puf-crVf_YvvT_SRepC_K9SQoFWsAXVDmIw</recordid><startdate>19790316</startdate><enddate>19790316</enddate><creator>Garnak, Margit</creator><creator>Reeves, Henry C.</creator><general>American Association for the Advancement of Science</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></search><sort><creationdate>19790316</creationdate><title>Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli</title><author>Garnak, Margit ; Reeves, Henry C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c307t-844a6a74928b8e435ad9c976aa17f4344b6da3221d469d18f972f06628359ae33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Acetates</topic><topic>Acetates - metabolism</topic><topic>Bacteria</topic><topic>Citrates</topic><topic>Dehydrogenases</topic><topic>Enzymes</topic><topic>Escherichia coli - enzymology</topic><topic>Gels</topic><topic>Isocitrate Dehydrogenase - metabolism</topic><topic>Isocitrates</topic><topic>NADP - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Radioactive decay</topic><topic>Serine - metabolism</topic><topic>Sodium</topic><topic>Threonine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Garnak, Margit</creatorcontrib><creatorcontrib>Reeves, Henry C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Garnak, Margit</au><au>Reeves, Henry C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1979-03-16</date><risdate>1979</risdate><volume>203</volume><issue>4385</issue><spage>1111</spage><epage>1112</epage><pages>1111-1112</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>34215</pmid><doi>10.1126/science.34215</doi><tpages>2</tpages></addata></record> |
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source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
subjects | Acetates Acetates - metabolism Bacteria Citrates Dehydrogenases Enzymes Escherichia coli - enzymology Gels Isocitrate Dehydrogenase - metabolism Isocitrates NADP - metabolism Phosphorylation Protein Kinases - metabolism Radioactive decay Serine - metabolism Sodium Threonine - metabolism |
title | Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli |
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