Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit
ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tiss...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2005-12, Vol.139 (4), p.1625-1634 |
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| creator | Linebarger, Carla R. Lyerly Boehlein, Susan K Sewell, Aileen K Shaw, Janine Hannah, L. Curtis |
| description | ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion of this motif into recombinant maize (Zea mays) endosperm AGPase increased the half-life at 58°C more than 70-fold. K[subscript m] values for physiological substrates were unaffected, although K[subscript cat] was doubled. A cysteine within the inserted motif gives rise to small subunit homodimers not found in the wild-type maize enzyme. Placement of this N-terminal motif into a mosaic small subunit containing the N terminus from maize endosperm and the C terminus from potato tuber AGPase increases heat stability more than 300-fold. |
| doi_str_mv | 10.1104/pp.105.067637 |
| format | Article |
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Lyerly ; Boehlein, Susan K ; Sewell, Aileen K ; Shaw, Janine ; Hannah, L. Curtis</creator><creatorcontrib>Linebarger, Carla R. Lyerly ; Boehlein, Susan K ; Sewell, Aileen K ; Shaw, Janine ; Hannah, L. Curtis</creatorcontrib><description>ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion of this motif into recombinant maize (Zea mays) endosperm AGPase increased the half-life at 58°C more than 70-fold. K[subscript m] values for physiological substrates were unaffected, although K[subscript cat] was doubled. A cysteine within the inserted motif gives rise to small subunit homodimers not found in the wild-type maize enzyme. Placement of this N-terminal motif into a mosaic small subunit containing the N terminus from maize endosperm and the C terminus from potato tuber AGPase increases heat stability more than 300-fold.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.105.067637</identifier><identifier>PMID: 16299180</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>ADP-glucose pyrophosphorylase ; Amino Acid Motifs ; Amino Acid Sequence ; amino acid sequences ; Amino acids ; Biochemical Processes and Macromolecular Structures ; Biological and medical sciences ; Corn ; cysteine ; Cysteine - chemistry ; Disulfides ; Endosperm ; enzyme activity ; Enzyme Stability ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gels ; Glucose-1-Phosphate Adenylyltransferase - chemistry ; Glucose-1-Phosphate Adenylyltransferase - genetics ; Glucose-1-Phosphate Adenylyltransferase - metabolism ; Hot Temperature ; insertional mutagenesis ; Kinetics ; Metabolism ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutagenesis, Site-Directed ; nucleotidyltransferases ; Photosynthesis, respiration. Anabolism, catabolism ; plant biochemistry ; plant genetics ; Plant physiology and development ; plant proteins ; Plants ; Plants, Genetically Modified ; Protein Structure, Quaternary ; Protein Subunits ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Starches ; thermal stability ; Tubers ; Zea mays ; Zea mays - enzymology ; Zea mays - genetics</subject><ispartof>Plant physiology (Bethesda), 2005-12, Vol.139 (4), p.1625-1634</ispartof><rights>Copyright 2005 American Society of Plant Biologists</rights><rights>2006 INIST-CNRS</rights><rights>Copyright © 2005, American Society of Plant Biologists 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-909354636da6fb35313580745187cb7cac7afff69e7e1fc2a5f97a87d3c5e4903</citedby><cites>FETCH-LOGICAL-c592t-909354636da6fb35313580745187cb7cac7afff69e7e1fc2a5f97a87d3c5e4903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4281991$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4281991$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17353197$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16299180$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Linebarger, Carla R. Lyerly</creatorcontrib><creatorcontrib>Boehlein, Susan K</creatorcontrib><creatorcontrib>Sewell, Aileen K</creatorcontrib><creatorcontrib>Shaw, Janine</creatorcontrib><creatorcontrib>Hannah, L. Curtis</creatorcontrib><title>Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion of this motif into recombinant maize (Zea mays) endosperm AGPase increased the half-life at 58°C more than 70-fold. K[subscript m] values for physiological substrates were unaffected, although K[subscript cat] was doubled. A cysteine within the inserted motif gives rise to small subunit homodimers not found in the wild-type maize enzyme. Placement of this N-terminal motif into a mosaic small subunit containing the N terminus from maize endosperm and the C terminus from potato tuber AGPase increases heat stability more than 300-fold.</description><subject>ADP-glucose pyrophosphorylase</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Biochemical Processes and Macromolecular Structures</subject><subject>Biological and medical sciences</subject><subject>Corn</subject><subject>cysteine</subject><subject>Cysteine - chemistry</subject><subject>Disulfides</subject><subject>Endosperm</subject><subject>enzyme activity</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Glucose-1-Phosphate Adenylyltransferase - chemistry</subject><subject>Glucose-1-Phosphate Adenylyltransferase - genetics</subject><subject>Glucose-1-Phosphate Adenylyltransferase - metabolism</subject><subject>Hot Temperature</subject><subject>insertional mutagenesis</subject><subject>Kinetics</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Insertional</subject><subject>Mutagenesis, Site-Directed</subject><subject>nucleotidyltransferases</subject><subject>Photosynthesis, respiration. Anabolism, catabolism</subject><subject>plant biochemistry</subject><subject>plant genetics</subject><subject>Plant physiology and development</subject><subject>plant proteins</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Subunits</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Starches</subject><subject>thermal stability</subject><subject>Tubers</subject><subject>Zea mays</subject><subject>Zea mays - enzymology</subject><subject>Zea mays - genetics</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVksFu1DAQhiMEokvhyA2BL3DLYsdx7FyQqqW0KxWotO3ZmnjtrqusndoOUngH3hlHu2rh5JH_T59HMy6KtwQvCcH152FYEsyWuOEN5c-KBWG0KitWi-fFAuNcYyHak-JVjPcYY0JJ_bI4IU3VtkTgRfHnUkNCmwSd7W2akDfoO9jfGp27rY-DDnt09vW6vOhH5aNG11Pwwy4HOx-mHvLNOmZ0B07pLeomtHZRh2S9m02AVlNM2jqNrENpp9EPdJOV1o1xzuebzR76Hm3GbnQ2vS5eGOijfnM8T4vbb-c3q8vy6ufFenV2VSrWVqlscUtZ3dBmC43pKKOEMoF5zYjgquMKFAdjTNNqrolRFTDTchB8SxXTdYvpafHl4B3Gbq-3SrsUoJdDsHsIk_Rg5f-Jszt553_JPD_Map4Fn46C4B9GHZPc26h034PTfoyyEULQSlQZLA-gCj7GoM3jIwTLeYFyGHLJ5GGBmX__b2dP9HFjGfh4BCAq6E3Io7fxiePzONpZ9O7A3cfkw2NeV4JkUY4_HGIDXsJdyIrbTZX_B8491Yw29C8FXbgA</recordid><startdate>20051201</startdate><enddate>20051201</enddate><creator>Linebarger, Carla R. 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Psychology</topic><topic>Gels</topic><topic>Glucose-1-Phosphate Adenylyltransferase - chemistry</topic><topic>Glucose-1-Phosphate Adenylyltransferase - genetics</topic><topic>Glucose-1-Phosphate Adenylyltransferase - metabolism</topic><topic>Hot Temperature</topic><topic>insertional mutagenesis</topic><topic>Kinetics</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Insertional</topic><topic>Mutagenesis, Site-Directed</topic><topic>nucleotidyltransferases</topic><topic>Photosynthesis, respiration. 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Curtis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2005-12-01</date><risdate>2005</risdate><volume>139</volume><issue>4</issue><spage>1625</spage><epage>1634</epage><pages>1625-1634</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion of this motif into recombinant maize (Zea mays) endosperm AGPase increased the half-life at 58°C more than 70-fold. K[subscript m] values for physiological substrates were unaffected, although K[subscript cat] was doubled. A cysteine within the inserted motif gives rise to small subunit homodimers not found in the wild-type maize enzyme. Placement of this N-terminal motif into a mosaic small subunit containing the N terminus from maize endosperm and the C terminus from potato tuber AGPase increases heat stability more than 300-fold.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>16299180</pmid><doi>10.1104/pp.105.067637</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0032-0889 |
| ispartof | Plant physiology (Bethesda), 2005-12, Vol.139 (4), p.1625-1634 |
| issn | 0032-0889 1532-2548 |
| language | eng |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | ADP-glucose pyrophosphorylase Amino Acid Motifs Amino Acid Sequence amino acid sequences Amino acids Biochemical Processes and Macromolecular Structures Biological and medical sciences Corn cysteine Cysteine - chemistry Disulfides Endosperm enzyme activity Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Gels Glucose-1-Phosphate Adenylyltransferase - chemistry Glucose-1-Phosphate Adenylyltransferase - genetics Glucose-1-Phosphate Adenylyltransferase - metabolism Hot Temperature insertional mutagenesis Kinetics Metabolism Molecular Sequence Data Mutagenesis, Insertional Mutagenesis, Site-Directed nucleotidyltransferases Photosynthesis, respiration. Anabolism, catabolism plant biochemistry plant genetics Plant physiology and development plant proteins Plants Plants, Genetically Modified Protein Structure, Quaternary Protein Subunits Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Starches thermal stability Tubers Zea mays Zea mays - enzymology Zea mays - genetics |
| title | Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit |
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