Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize
The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg 2+. The lag time as a function of substrate concentration...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1990-02, Vol.277 (1), p.69-73 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 73 |
|---|---|
| container_issue | 1 |
| container_start_page | 69 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 277 |
| creator | Jawali, Narendra |
| description | The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg
2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady state, cooperative kinetics for Mg
2+ was changed to hyperbolic kinetics in the presence of 2-PG. Studies on the equilibrium binding of Mg
2+ with the help of an external fluorescent probe, 8-anilino-6-naphthalinosulfonate showed that the hyperbolic binding of Mg
2+ was changed to cooperative binding in the presence of 2-PG. On the basis of these results along with the results presented in the preceding paper, a fully concerted sequential model with subunit interaction is proposed for PEPC. |
| doi_str_mv | 10.1016/0003-9861(90)90551-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79650350</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0003986190905519</els_id><sourcerecordid>15599452</sourcerecordid><originalsourceid>FETCH-LOGICAL-c437t-773248f2eed883c4ded864a294c31201566ad078d08ca1a7668fbd2cd448d8833</originalsourceid><addsrcrecordid>eNqFkF1rFDEUhoModfvxB0Rhbix6Me3Jx2SSG6EUdYWCF7bXIZuc0cjMZE1miuuvb6a71DuFhAN5n_MSHkJeU7igQOUlAPBaK0nfaXivoWlorZ-RFQUta-BKPCerJ-QlOc75JwClQrIjcsQ4SMrkiqzXuzxhwim4arTTnLCKXbX9EXO5OMZ-u0vzvZ2wcjZt4u9dbzNWIce-vPmqS3GoBhv-4Cl50dk-49lhnpC7Tx9vr9f1zdfPX66vbmoneDvVbcuZUB1D9EpxJ3yZUlimheOUAW2ktB5a5UE5S20rpeo2njkvhFo2-Ak53_duU_w1Y57MELLDvrcjxjmbVssGeDn_A2nTaC0aVkCxB12KOSfszDaFwaadoWAW02bRaBaNRoN5NG10WXtz6J83A_qnpYPakr895DY723fJji7kv926UVropefVnutsNPZ7KszdNw2sVaBK-GEfYlF6HzCZ7AKODn1I6CbjY_j3Lx8A65CiLQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15599452</pqid></control><display><type>article</type><title>Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Jawali, Narendra</creator><creatorcontrib>Jawali, Narendra</creatorcontrib><description>The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg
2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady state, cooperative kinetics for Mg
2+ was changed to hyperbolic kinetics in the presence of 2-PG. Studies on the equilibrium binding of Mg
2+ with the help of an external fluorescent probe, 8-anilino-6-naphthalinosulfonate showed that the hyperbolic binding of Mg
2+ was changed to cooperative binding in the presence of 2-PG. On the basis of these results along with the results presented in the preceding paper, a fully concerted sequential model with subunit interaction is proposed for PEPC.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(90)90551-9</identifier><identifier>PMID: 2306126</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Carboxy-Lyases - metabolism ; ENZYME KINETICS ; ENZYME MECHANISMS ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Kinetics ; LIASAS ; Ligands ; LYASE ; LYASES ; Macromolecular Substances ; MAGNESIO ; MAGNESIUM ; Magnesium Chloride - pharmacology ; Models, Structural ; Models, Theoretical ; Phosphoenolpyruvate Carboxylase - isolation & purification ; Phosphoenolpyruvate Carboxylase - metabolism ; Spectrometry, Fluorescence ; SUBUNIT INTERACTION ; ZEA MAYS ; Zea mays - enzymology</subject><ispartof>Archives of biochemistry and biophysics, 1990-02, Vol.277 (1), p.69-73</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-773248f2eed883c4ded864a294c31201566ad078d08ca1a7668fbd2cd448d8833</citedby><cites>FETCH-LOGICAL-c437t-773248f2eed883c4ded864a294c31201566ad078d08ca1a7668fbd2cd448d8833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986190905519$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19589499$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2306126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jawali, Narendra</creatorcontrib><title>Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg
2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady state, cooperative kinetics for Mg
2+ was changed to hyperbolic kinetics in the presence of 2-PG. Studies on the equilibrium binding of Mg
2+ with the help of an external fluorescent probe, 8-anilino-6-naphthalinosulfonate showed that the hyperbolic binding of Mg
2+ was changed to cooperative binding in the presence of 2-PG. On the basis of these results along with the results presented in the preceding paper, a fully concerted sequential model with subunit interaction is proposed for PEPC.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carboxy-Lyases - metabolism</subject><subject>ENZYME KINETICS</subject><subject>ENZYME MECHANISMS</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>LIASAS</subject><subject>Ligands</subject><subject>LYASE</subject><subject>LYASES</subject><subject>Macromolecular Substances</subject><subject>MAGNESIO</subject><subject>MAGNESIUM</subject><subject>Magnesium Chloride - pharmacology</subject><subject>Models, Structural</subject><subject>Models, Theoretical</subject><subject>Phosphoenolpyruvate Carboxylase - isolation & purification</subject><subject>Phosphoenolpyruvate Carboxylase - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>SUBUNIT INTERACTION</subject><subject>ZEA MAYS</subject><subject>Zea mays - enzymology</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF1rFDEUhoModfvxB0Rhbix6Me3Jx2SSG6EUdYWCF7bXIZuc0cjMZE1miuuvb6a71DuFhAN5n_MSHkJeU7igQOUlAPBaK0nfaXivoWlorZ-RFQUta-BKPCerJ-QlOc75JwClQrIjcsQ4SMrkiqzXuzxhwim4arTTnLCKXbX9EXO5OMZ-u0vzvZ2wcjZt4u9dbzNWIce-vPmqS3GoBhv-4Cl50dk-49lhnpC7Tx9vr9f1zdfPX66vbmoneDvVbcuZUB1D9EpxJ3yZUlimheOUAW2ktB5a5UE5S20rpeo2njkvhFo2-Ak53_duU_w1Y57MELLDvrcjxjmbVssGeDn_A2nTaC0aVkCxB12KOSfszDaFwaadoWAW02bRaBaNRoN5NG10WXtz6J83A_qnpYPakr895DY723fJji7kv926UVropefVnutsNPZ7KszdNw2sVaBK-GEfYlF6HzCZ7AKODn1I6CbjY_j3Lx8A65CiLQ</recordid><startdate>19900215</startdate><enddate>19900215</enddate><creator>Jawali, Narendra</creator><general>Elsevier Inc</general><general>Elsevier</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>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900215</creationdate><title>Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize</title><author>Jawali, Narendra</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-773248f2eed883c4ded864a294c31201566ad078d08ca1a7668fbd2cd448d8833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carboxy-Lyases - metabolism</topic><topic>ENZYME KINETICS</topic><topic>ENZYME MECHANISMS</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>LIASAS</topic><topic>Ligands</topic><topic>LYASE</topic><topic>LYASES</topic><topic>Macromolecular Substances</topic><topic>MAGNESIO</topic><topic>MAGNESIUM</topic><topic>Magnesium Chloride - pharmacology</topic><topic>Models, Structural</topic><topic>Models, Theoretical</topic><topic>Phosphoenolpyruvate Carboxylase - isolation & purification</topic><topic>Phosphoenolpyruvate Carboxylase - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>SUBUNIT INTERACTION</topic><topic>ZEA MAYS</topic><topic>Zea mays - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jawali, Narendra</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>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jawali, Narendra</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1990-02-15</date><risdate>1990</risdate><volume>277</volume><issue>1</issue><spage>69</spage><epage>73</epage><pages>69-73</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg
2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady state, cooperative kinetics for Mg
2+ was changed to hyperbolic kinetics in the presence of 2-PG. Studies on the equilibrium binding of Mg
2+ with the help of an external fluorescent probe, 8-anilino-6-naphthalinosulfonate showed that the hyperbolic binding of Mg
2+ was changed to cooperative binding in the presence of 2-PG. On the basis of these results along with the results presented in the preceding paper, a fully concerted sequential model with subunit interaction is proposed for PEPC.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2306126</pmid><doi>10.1016/0003-9861(90)90551-9</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1990-02, Vol.277 (1), p.69-73 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79650350 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Analytical, structural and metabolic biochemistry Biological and medical sciences Carboxy-Lyases - metabolism ENZYME KINETICS ENZYME MECHANISMS Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics LIASAS Ligands LYASE LYASES Macromolecular Substances MAGNESIO MAGNESIUM Magnesium Chloride - pharmacology Models, Structural Models, Theoretical Phosphoenolpyruvate Carboxylase - isolation & purification Phosphoenolpyruvate Carboxylase - metabolism Spectrometry, Fluorescence SUBUNIT INTERACTION ZEA MAYS Zea mays - enzymology |
| title | Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T01%3A41%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Hysteretic%20nature%20of%20phosphoenolpyruvate%20carboxylase%20isolated%20from%20maize&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Jawali,%20Narendra&rft.date=1990-02-15&rft.volume=277&rft.issue=1&rft.spage=69&rft.epage=73&rft.pages=69-73&rft.issn=0003-9861&rft.eissn=1096-0384&rft.coden=ABBIA4&rft_id=info:doi/10.1016/0003-9861(90)90551-9&rft_dat=%3Cproquest_cross%3E15599452%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15599452&rft_id=info:pmid/2306126&rft_els_id=0003986190905519&rfr_iscdi=true |