Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry
•Substrate binding properties of potato AGPase variants were analyzed by ITC.•The heterotetrameric AGPase, SWTLWT, displays two binding sites for ATP.•The homotetrameric enzymes, SS and LS, contain only a single binding site for ATP.•SWTLWT exhibits higher affinity to ATP due to synergistic interact...
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| Veröffentlicht in: | FEBS letters 2015-06, Vol.589 (13), p.1444-1449 |
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| creator | Cakir, Bilal Tuncel, Aytug Green, Abigail R. Koper, Kaan Hwang, Seon-Kap Okita, Thomas W. Kang, ChulHee |
| description | •Substrate binding properties of potato AGPase variants were analyzed by ITC.•The heterotetrameric AGPase, SWTLWT, displays two binding sites for ATP.•The homotetrameric enzymes, SS and LS, contain only a single binding site for ATP.•SWTLWT exhibits higher affinity to ATP due to synergistic interaction of LS and SS.•AGPase does not bind glucose 1-phosphate in the presence or absence of ATPγS.
Substrate binding properties of the large (LS) and small (SS) subunits of potato tuber ADP-glucose pyrophosphorylase were investigated by using isothermal titration calorimetry. Our results clearly show that the wild type heterotetramer (SWTLWT) possesses two distinct types of ATP binding sites, whereas the homotetrameric LS and SS variant forms only exhibited properties of one of the two binding sites. The wild type enzyme also exhibited significantly increased affinity to this substrate compared to the homotetrameric enzyme forms. No stable binding was evident for the second substrate, glucose-1-phosphate, in the presence or absence of ATPγS suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell–Chance bi bi reaction mechanism. |
| doi_str_mv | 10.1016/j.febslet.2015.04.042 |
| format | Article |
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Substrate binding properties of the large (LS) and small (SS) subunits of potato tuber ADP-glucose pyrophosphorylase were investigated by using isothermal titration calorimetry. Our results clearly show that the wild type heterotetramer (SWTLWT) possesses two distinct types of ATP binding sites, whereas the homotetrameric LS and SS variant forms only exhibited properties of one of the two binding sites. The wild type enzyme also exhibited significantly increased affinity to this substrate compared to the homotetrameric enzyme forms. No stable binding was evident for the second substrate, glucose-1-phosphate, in the presence or absence of ATPγS suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell–Chance bi bi reaction mechanism.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2015.04.042</identifier><identifier>PMID: 25953126</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Adenosine Triphosphate - analogs & derivatives ; Adenosine Triphosphate - chemistry ; Adenosine Triphosphate - metabolism ; ADP-glucose pyrophosphorylase ; Binding Sites ; Binding, Competitive ; Blotting, Western ; Calorimetry - methods ; Glucose-1-Phosphate Adenylyltransferase - chemistry ; Glucose-1-Phosphate Adenylyltransferase - metabolism ; Glucosephosphates - chemistry ; Glucosephosphates - metabolism ; Heterotetramer ; Homotetramer ; Isothermal titration calorimetry ; Kinetics ; Models, Molecular ; Molecular Structure ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plant Tubers - enzymology ; Protein Binding ; Protein Multimerization ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Solanum tuberosum - enzymology ; Starch synthesis ; Substrate binding properties ; Substrate Specificity ; Thermodynamics</subject><ispartof>FEBS letters, 2015-06, Vol.589 (13), p.1444-1449</ispartof><rights>2015 Federation of European Biochemical Societies</rights><rights>FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5472-28d586150bb74175f72a0861d8542349942324ba0003727cd957a6161faa42643</citedby><cites>FETCH-LOGICAL-c5472-28d586150bb74175f72a0861d8542349942324ba0003727cd957a6161faa42643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2015.04.042$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2015.04.042$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25953126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cakir, Bilal</creatorcontrib><creatorcontrib>Tuncel, Aytug</creatorcontrib><creatorcontrib>Green, Abigail R.</creatorcontrib><creatorcontrib>Koper, Kaan</creatorcontrib><creatorcontrib>Hwang, Seon-Kap</creatorcontrib><creatorcontrib>Okita, Thomas W.</creatorcontrib><creatorcontrib>Kang, ChulHee</creatorcontrib><title>Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•Substrate binding properties of potato AGPase variants were analyzed by ITC.•The heterotetrameric AGPase, SWTLWT, displays two binding sites for ATP.•The homotetrameric enzymes, SS and LS, contain only a single binding site for ATP.•SWTLWT exhibits higher affinity to ATP due to synergistic interaction of LS and SS.•AGPase does not bind glucose 1-phosphate in the presence or absence of ATPγS.
Substrate binding properties of the large (LS) and small (SS) subunits of potato tuber ADP-glucose pyrophosphorylase were investigated by using isothermal titration calorimetry. Our results clearly show that the wild type heterotetramer (SWTLWT) possesses two distinct types of ATP binding sites, whereas the homotetrameric LS and SS variant forms only exhibited properties of one of the two binding sites. The wild type enzyme also exhibited significantly increased affinity to this substrate compared to the homotetrameric enzyme forms. No stable binding was evident for the second substrate, glucose-1-phosphate, in the presence or absence of ATPγS suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell–Chance bi bi reaction mechanism.</description><subject>Adenosine Triphosphate - analogs & derivatives</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>ADP-glucose pyrophosphorylase</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Blotting, Western</subject><subject>Calorimetry - methods</subject><subject>Glucose-1-Phosphate Adenylyltransferase - chemistry</subject><subject>Glucose-1-Phosphate Adenylyltransferase - metabolism</subject><subject>Glucosephosphates - chemistry</subject><subject>Glucosephosphates - metabolism</subject><subject>Heterotetramer</subject><subject>Homotetramer</subject><subject>Isothermal titration calorimetry</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Tubers - enzymology</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>Solanum tuberosum - enzymology</subject><subject>Starch synthesis</subject><subject>Substrate binding properties</subject><subject>Substrate Specificity</subject><subject>Thermodynamics</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUU1v1DAQtRCILoWfAPKRSxZ_xskJldLSSpVaqXC27GTSeuWNg-0UReLH42gXrkUaezSjN29m3iD0npItJbT-tNsOYJOHvGWEyi0RxdgLtKGN4hUXdfMSbQihopKq5SfoTUo7UuKGtq_RCZOt5JTVG_T7frYpR5MBWzf2bnzAUwwTxOwg4TDgKWSTA86zhYjPvt5VD37uQgI8LQX3GFJ5cfGmZEzCPWSIezdCj-2CXQr5scTG4-zWJi6MuDM-RLeHHJe36NVgfIJ3R3-KflxefD-_qm5uv12fn91UnRSKVazpZVNTSaxVgio5KGZISfSNFIyLti0_E9aU_bhiqutbqUxNazoYI1gt-Cn6eOAtq_2cIWW9d6kD780IYU6a1g0nqpFMFag8QLsYUoow6KkMa-KiKdGr8Hqnj8LrVXhNRDFW6j4cW8x2D_2_qr9KF8DVAfDLeVj-j1VfXnxh9-sV1yMWAQgnZO31-UAFRbMnB1GnzsHYQe8idFn3wT0z7R9xj62-</recordid><startdate>20150604</startdate><enddate>20150604</enddate><creator>Cakir, Bilal</creator><creator>Tuncel, Aytug</creator><creator>Green, Abigail R.</creator><creator>Koper, Kaan</creator><creator>Hwang, Seon-Kap</creator><creator>Okita, Thomas W.</creator><creator>Kang, ChulHee</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20150604</creationdate><title>Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry</title><author>Cakir, Bilal ; Tuncel, Aytug ; Green, Abigail R. ; Koper, Kaan ; Hwang, Seon-Kap ; Okita, Thomas W. ; Kang, ChulHee</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5472-28d586150bb74175f72a0861d8542349942324ba0003727cd957a6161faa42643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Adenosine Triphosphate - analogs & derivatives</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>ADP-glucose pyrophosphorylase</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Blotting, Western</topic><topic>Calorimetry - methods</topic><topic>Glucose-1-Phosphate Adenylyltransferase - chemistry</topic><topic>Glucose-1-Phosphate Adenylyltransferase - metabolism</topic><topic>Glucosephosphates - chemistry</topic><topic>Glucosephosphates - metabolism</topic><topic>Heterotetramer</topic><topic>Homotetramer</topic><topic>Isothermal titration calorimetry</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Tubers - enzymology</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - metabolism</topic><topic>Solanum tuberosum - enzymology</topic><topic>Starch synthesis</topic><topic>Substrate binding properties</topic><topic>Substrate Specificity</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cakir, Bilal</creatorcontrib><creatorcontrib>Tuncel, Aytug</creatorcontrib><creatorcontrib>Green, Abigail R.</creatorcontrib><creatorcontrib>Koper, Kaan</creatorcontrib><creatorcontrib>Hwang, Seon-Kap</creatorcontrib><creatorcontrib>Okita, Thomas W.</creatorcontrib><creatorcontrib>Kang, ChulHee</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cakir, Bilal</au><au>Tuncel, Aytug</au><au>Green, Abigail R.</au><au>Koper, Kaan</au><au>Hwang, Seon-Kap</au><au>Okita, Thomas W.</au><au>Kang, ChulHee</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2015-06-04</date><risdate>2015</risdate><volume>589</volume><issue>13</issue><spage>1444</spage><epage>1449</epage><pages>1444-1449</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•Substrate binding properties of potato AGPase variants were analyzed by ITC.•The heterotetrameric AGPase, SWTLWT, displays two binding sites for ATP.•The homotetrameric enzymes, SS and LS, contain only a single binding site for ATP.•SWTLWT exhibits higher affinity to ATP due to synergistic interaction of LS and SS.•AGPase does not bind glucose 1-phosphate in the presence or absence of ATPγS.
Substrate binding properties of the large (LS) and small (SS) subunits of potato tuber ADP-glucose pyrophosphorylase were investigated by using isothermal titration calorimetry. Our results clearly show that the wild type heterotetramer (SWTLWT) possesses two distinct types of ATP binding sites, whereas the homotetrameric LS and SS variant forms only exhibited properties of one of the two binding sites. The wild type enzyme also exhibited significantly increased affinity to this substrate compared to the homotetrameric enzyme forms. No stable binding was evident for the second substrate, glucose-1-phosphate, in the presence or absence of ATPγS suggesting that interaction of glucose-1-phosphate is dependent on hydrolysis of ATP and supports the Theorell–Chance bi bi reaction mechanism.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>25953126</pmid><doi>10.1016/j.febslet.2015.04.042</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ADP-glucose pyrophosphorylase Binding Sites Binding, Competitive Blotting, Western Calorimetry - methods Glucose-1-Phosphate Adenylyltransferase - chemistry Glucose-1-Phosphate Adenylyltransferase - metabolism Glucosephosphates - chemistry Glucosephosphates - metabolism Heterotetramer Homotetramer Isothermal titration calorimetry Kinetics Models, Molecular Molecular Structure Plant Proteins - chemistry Plant Proteins - metabolism Plant Tubers - enzymology Protein Binding Protein Multimerization Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - metabolism Solanum tuberosum - enzymology Starch synthesis Substrate binding properties Substrate Specificity Thermodynamics |
| title | Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry |
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