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Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms
Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds ( Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min −1 mg −1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphory...
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| Published in: | Biochimie 2010-10, Vol.92 (10), p.1362-1370 |
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| Main Authors: | , , , |
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| container_title | Biochimie |
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| creator | Černý, Martin Doubnerová, Veronika Müller, Karel Ryšlavá, Helena |
| description | Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds (
Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min
−1 mg
−1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to
l-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition. |
| doi_str_mv | 10.1016/j.biochi.2010.06.019 |
| format | article |
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Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min
−1 mg
−1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to
l-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2010.06.019</identifier><identifier>PMID: 20600561</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Animals ; Cattle ; Cyclic AMP-Dependent Protein Kinases - pharmacology ; Kinetics ; Malates - pharmacology ; Phosphoenolpyruvate carboxylase ; Phosphoenolpyruvate Carboxylase - antagonists & inhibitors ; Phosphoenolpyruvate Carboxylase - isolation & purification ; Phosphoenolpyruvate Carboxylase - metabolism ; Phosphorylation ; Seed ; Seeds - enzymology ; Sigmoidal kinetics ; Zea mays ; Zea mays - enzymology</subject><ispartof>Biochimie, 2010-10, Vol.92 (10), p.1362-1370</ispartof><rights>2010 Elsevier Masson SAS</rights><rights>Copyright © 2010 Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-e5a86170345e21a070531237e44b4bb92956ffb8e568063f3dacf1def81fa5e23</citedby><cites>FETCH-LOGICAL-c427t-e5a86170345e21a070531237e44b4bb92956ffb8e568063f3dacf1def81fa5e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20600561$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Černý, Martin</creatorcontrib><creatorcontrib>Doubnerová, Veronika</creatorcontrib><creatorcontrib>Müller, Karel</creatorcontrib><creatorcontrib>Ryšlavá, Helena</creatorcontrib><title>Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds (
Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min
−1 mg
−1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to
l-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition.</description><subject>Animals</subject><subject>Cattle</subject><subject>Cyclic AMP-Dependent Protein Kinases - pharmacology</subject><subject>Kinetics</subject><subject>Malates - pharmacology</subject><subject>Phosphoenolpyruvate carboxylase</subject><subject>Phosphoenolpyruvate Carboxylase - antagonists & inhibitors</subject><subject>Phosphoenolpyruvate Carboxylase - isolation & purification</subject><subject>Phosphoenolpyruvate Carboxylase - metabolism</subject><subject>Phosphorylation</subject><subject>Seed</subject><subject>Seeds - enzymology</subject><subject>Sigmoidal kinetics</subject><subject>Zea mays</subject><subject>Zea mays - enzymology</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp9kEFr3DAQhUVJabZp_0EpuuXk7ciyZbuHQFiSJhBoDulZyNKI1WJbjiSHbM754VXYNJQeehhmGN6bx3yEfGGwZsDEt926d15v3bqEvAKxBta9IysmeFsI1vIjsgIOUHTQVsfkY4w7AKih7D6Q4xJEngVbkefNVgWlEwb3pJLzE_WWzlsfc-Hkh3kflgeVkGoVev-4H1REaoMf6ajSEjA394Q0Ipr4nd4GP2NIDuNfZ0I2JTRUTYYa_GdpfRjjJ_LeqiHi59d-Qn5dXtxtroqbnz-uN-c3ha7KJhVYq1awBnhVY8kUNFBzVvIGq6qv-r4ru1pY27dYixYEt9wobZlB2zKrsoWfkNPD3Tn4-wVjkqOLGodBTeiXKJtacGhzQFZWB6UOPsaAVs7BjSrsJQP5gl_u5AG_fMEvQciMP9u-vgYs_YjmzfSHdxacHQSY33xwGGTUDieNxgXUSRrv_p_wG3yFnDM</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Černý, Martin</creator><creator>Doubnerová, Veronika</creator><creator>Müller, Karel</creator><creator>Ryšlavá, Helena</creator><general>Elsevier Masson SAS</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><scope>7X8</scope></search><sort><creationdate>20101001</creationdate><title>Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms</title><author>Černý, Martin ; Doubnerová, Veronika ; Müller, Karel ; Ryšlavá, Helena</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-e5a86170345e21a070531237e44b4bb92956ffb8e568063f3dacf1def81fa5e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Cyclic AMP-Dependent Protein Kinases - pharmacology</topic><topic>Kinetics</topic><topic>Malates - pharmacology</topic><topic>Phosphoenolpyruvate carboxylase</topic><topic>Phosphoenolpyruvate Carboxylase - antagonists & inhibitors</topic><topic>Phosphoenolpyruvate Carboxylase - isolation & purification</topic><topic>Phosphoenolpyruvate Carboxylase - metabolism</topic><topic>Phosphorylation</topic><topic>Seed</topic><topic>Seeds - enzymology</topic><topic>Sigmoidal kinetics</topic><topic>Zea mays</topic><topic>Zea mays - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Černý, Martin</creatorcontrib><creatorcontrib>Doubnerová, Veronika</creatorcontrib><creatorcontrib>Müller, Karel</creatorcontrib><creatorcontrib>Ryšlavá, Helena</creatorcontrib><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>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Černý, Martin</au><au>Doubnerová, Veronika</au><au>Müller, Karel</au><au>Ryšlavá, Helena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2010-10-01</date><risdate>2010</risdate><volume>92</volume><issue>10</issue><spage>1362</spage><epage>1370</epage><pages>1362-1370</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds (
Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min
−1 mg
−1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to
l-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>20600561</pmid><doi>10.1016/j.biochi.2010.06.019</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 2010-10, Vol.92 (10), p.1362-1370 |
| issn | 0300-9084 1638-6183 |
| language | eng |
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| source | ScienceDirect Journals |
| subjects | Animals Cattle Cyclic AMP-Dependent Protein Kinases - pharmacology Kinetics Malates - pharmacology Phosphoenolpyruvate carboxylase Phosphoenolpyruvate Carboxylase - antagonists & inhibitors Phosphoenolpyruvate Carboxylase - isolation & purification Phosphoenolpyruvate Carboxylase - metabolism Phosphorylation Seed Seeds - enzymology Sigmoidal kinetics Zea mays Zea mays - enzymology |
| title | Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms |
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