cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase
The cooperative binding of the allosteric activator fructose-1,6-bisphosphate [Fru(1,6)P2] to yeast pyruvate kinase was investigated by equilibrium dialysis and fluorescence quench titration. The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed...
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| Veröffentlicht in: | The EMBO journal 1992-11, Vol.11 (11), p.3811-3814 |
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| creator | Murcott, T.H.L Gutfreund, H Muirhead, H |
| description | The cooperative binding of the allosteric activator fructose-1,6-bisphosphate [Fru(1,6)P2] to yeast pyruvate kinase was investigated by equilibrium dialysis and fluorescence quench titration. The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed fluorescence quench follows the binding of the ligand and not the cooperative T to R state transition. Additionally it is shown that the binding of Fru(1,6)P2 to yeast pyruvate kinase is compatible with the model of cooperativity that has been proposed and incorporates an intermediate state, R', with properties between those of the T and R states. |
| doi_str_mv | 10.1002/j.1460-2075.1992.tb05472.x |
| format | Article |
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The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed fluorescence quench follows the binding of the ligand and not the cooperative T to R state transition. Additionally it is shown that the binding of Fru(1,6)P2 to yeast pyruvate kinase is compatible with the model of cooperativity that has been proposed and incorporates an intermediate state, R', with properties between those of the T and R states.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1992.tb05472.x</identifier><identifier>PMID: 1396575</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Allosteric Regulation ; Allosteric Site ; Analytical, structural and metabolic biochemistry ; binding ; binding sites ; Biological and medical sciences ; cooperative ; Dialysis ; enzyme activity ; Enzymes and enzyme inhibitors ; fructose ; fructose-1,6-bisphosphate ; Fructosediphosphates - metabolism ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Models, Molecular ; molecular conformation ; Protein Binding ; Protein Conformation ; pyruvate kinase ; Pyruvate Kinase - metabolism ; Regression Analysis ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Spectrometry, Fluorescence ; sugar phosphates ; Transferases</subject><ispartof>The EMBO journal, 1992-11, Vol.11 (11), p.3811-3814</ispartof><rights>1992 European Molecular Biology Organization</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5622-91531343b2b8258eaf9a52263f2313bd59ed095442fdd6ca7530def63c105a1a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC556889/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC556889/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5572891$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1396575$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murcott, T.H.L</creatorcontrib><creatorcontrib>Gutfreund, H</creatorcontrib><creatorcontrib>Muirhead, H</creatorcontrib><title>cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>The cooperative binding of the allosteric activator fructose-1,6-bisphosphate [Fru(1,6)P2] to yeast pyruvate kinase was investigated by equilibrium dialysis and fluorescence quench titration. The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed fluorescence quench follows the binding of the ligand and not the cooperative T to R state transition. Additionally it is shown that the binding of Fru(1,6)P2 to yeast pyruvate kinase is compatible with the model of cooperativity that has been proposed and incorporates an intermediate state, R', with properties between those of the T and R states.</description><subject>Allosteric Regulation</subject><subject>Allosteric Site</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>binding</subject><subject>binding sites</subject><subject>Biological and medical sciences</subject><subject>cooperative</subject><subject>Dialysis</subject><subject>enzyme activity</subject><subject>Enzymes and enzyme inhibitors</subject><subject>fructose</subject><subject>fructose-1,6-bisphosphate</subject><subject>Fructosediphosphates - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>molecular conformation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>pyruvate kinase</subject><subject>Pyruvate Kinase - metabolism</subject><subject>Regression Analysis</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Spectrometry, Fluorescence</subject><subject>sugar phosphates</subject><subject>Transferases</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkU2P1CAYx4nRrOPqRzA2xniylQcKLZt4WDerrlnjQfdMKIVZxk6p0I47315qJ6OejAcCef4vQH4IPQdcAMbk9aaAkuOc4IoVIAQpxgazsiLF3T20Okr30QoTDnkJtXiIHsW4wRizuoITdAJUcFaxFbrS3g8mqNHtTNa4vnX9OvM2s2HSo48mh1c8b1wcbn1aajTZ6LO9UXHMhn2YdvPkm-tVNI_RA6u6aJ4c9lN08-7y68WH_Prz-6uL8-tcM05ILoBRoCVtSFMTVhtlhWKEcGpJmjctE6bFgpUlsW3LtaoYxa2xnGrATIGip-jN0jtMzda02vRjUJ0cgtuqsJdeOfm30rtbufY7yRiva5HyLw_54L9PJo5y66I2Xad646coK0qAV0D_aQReUsEwTsazxaiDjzEYe3wMYDkDkxs5U5EzFTkDkwdg8i6Fn_75nd_RhVDSXxx0FbXqbFC9dvFoY6witYBkO19sP1xn9v_xAHn56e3HX-fU8WzpsMpLtQ7pmpsvBAPFUHGaCuhPige9BQ</recordid><startdate>199211</startdate><enddate>199211</enddate><creator>Murcott, T.H.L</creator><creator>Gutfreund, H</creator><creator>Muirhead, H</creator><general>Nature Publishing Group</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199211</creationdate><title>cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase</title><author>Murcott, T.H.L ; Gutfreund, H ; Muirhead, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5622-91531343b2b8258eaf9a52263f2313bd59ed095442fdd6ca7530def63c105a1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Allosteric Regulation</topic><topic>Allosteric Site</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>binding</topic><topic>binding sites</topic><topic>Biological and medical sciences</topic><topic>cooperative</topic><topic>Dialysis</topic><topic>enzyme activity</topic><topic>Enzymes and enzyme inhibitors</topic><topic>fructose</topic><topic>fructose-1,6-bisphosphate</topic><topic>Fructosediphosphates - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>molecular conformation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>pyruvate kinase</topic><topic>Pyruvate Kinase - metabolism</topic><topic>Regression Analysis</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Spectrometry, Fluorescence</topic><topic>sugar phosphates</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murcott, T.H.L</creatorcontrib><creatorcontrib>Gutfreund, H</creatorcontrib><creatorcontrib>Muirhead, H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murcott, T.H.L</au><au>Gutfreund, H</au><au>Muirhead, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1992-11</date><risdate>1992</risdate><volume>11</volume><issue>11</issue><spage>3811</spage><epage>3814</epage><pages>3811-3814</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The cooperative binding of the allosteric activator fructose-1,6-bisphosphate [Fru(1,6)P2] to yeast pyruvate kinase was investigated by equilibrium dialysis and fluorescence quench titration. The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed fluorescence quench follows the binding of the ligand and not the cooperative T to R state transition. Additionally it is shown that the binding of Fru(1,6)P2 to yeast pyruvate kinase is compatible with the model of cooperativity that has been proposed and incorporates an intermediate state, R', with properties between those of the T and R states.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>1396575</pmid><doi>10.1002/j.1460-2075.1992.tb05472.x</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Allosteric Regulation Allosteric Site Analytical, structural and metabolic biochemistry binding binding sites Biological and medical sciences cooperative Dialysis enzyme activity Enzymes and enzyme inhibitors fructose fructose-1,6-bisphosphate Fructosediphosphates - metabolism Fundamental and applied biological sciences. Psychology Kinetics Models, Molecular molecular conformation Protein Binding Protein Conformation pyruvate kinase Pyruvate Kinase - metabolism Regression Analysis Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Spectrometry, Fluorescence sugar phosphates Transferases |
| title | cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase |
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