Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves
Barley (Hordeum vulgare, cv. Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 an...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-03, Vol.268 (9), p.6228-6233 |
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| creator | Kleczkowski, L.A Villand, P Preiss, J Olsen, O.A |
| description | Barley (Hordeum vulgare, cv. Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 and 54 kDa, which were recognized by the respective rabbit antibodies against the small and/or large subunit of spinach leaf AGP. Substrate kinetics and product inhibition studies, carried out in the direction of ADP-glucose synthesis, suggested a sequential Iso Ordered Bi Bi kinetic mechanism for the enzyme. In addition, inhibition patterns with CrATP, a dead-end inhibitor of ATP-utilizing enzymes, were consistent with ATP (synthesis reaction) and ADP-glucose (pyrophosphorolysis reaction) binding first to different free forms of the enzyme. The AGP was potently activated by 3-phosphoglycerate (PGA) (K(a) of 5 micromolar) and inhibited by orthophosphate (P(i)), with the ratio of the two effectors playing a major role in modulating AGP activity. At low [PGA]/[P(i)] ratios, P(i) could reverse the activating effect of PGA. However, at the [PGA]/[P(i)] ratios of 1.4, or higher, some activating effect of P(i) in the presence of PGA was observed. PGA decreased the Km values for all substrates of AGP (in both the synthesis and pyrophosphorolysis directions). Properties of the barley leaf AGP are compared to those of AGP from barley seed endosperm, which is insensitive to PGA/P(i) regulation |
| doi_str_mv | 10.1016/S0021-9258(18)53243-9 |
| format | Article |
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Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 and 54 kDa, which were recognized by the respective rabbit antibodies against the small and/or large subunit of spinach leaf AGP. Substrate kinetics and product inhibition studies, carried out in the direction of ADP-glucose synthesis, suggested a sequential Iso Ordered Bi Bi kinetic mechanism for the enzyme. In addition, inhibition patterns with CrATP, a dead-end inhibitor of ATP-utilizing enzymes, were consistent with ATP (synthesis reaction) and ADP-glucose (pyrophosphorolysis reaction) binding first to different free forms of the enzyme. The AGP was potently activated by 3-phosphoglycerate (PGA) (K(a) of 5 micromolar) and inhibited by orthophosphate (P(i)), with the ratio of the two effectors playing a major role in modulating AGP activity. At low [PGA]/[P(i)] ratios, P(i) could reverse the activating effect of PGA. However, at the [PGA]/[P(i)] ratios of 1.4, or higher, some activating effect of P(i) in the presence of PGA was observed. PGA decreased the Km values for all substrates of AGP (in both the synthesis and pyrophosphorolysis directions). Properties of the barley leaf AGP are compared to those of AGP from barley seed endosperm, which is insensitive to PGA/P(i) regulation</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)53243-9</identifier><identifier>PMID: 8384204</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ADENOSINDIFOSFATO ; ADENOSINE DIPHOSPHATE ; Adenosine Triphosphate - metabolism ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Electrophoresis, Polyacrylamide Gel ; enzymatic activity ; Enzyme Activation ; Enzymes and enzyme inhibitors ; ESTER ; ESTERES ; FEUILLE ; FOSFATOS ; Fundamental and applied biological sciences. Psychology ; GLUCOSA ; GLUCOSE ; Glucose-1-Phosphate Adenylyltransferase ; Glyceric Acids - metabolism ; HOJAS ; Hordeum - enzymology ; HORDEUM VULGARE ; INHIBIDORES DE ENZIMAS ; INHIBITEUR D'ENZYME ; Kinetics ; Nucleotidyltransferases - antagonists & inhibitors ; Nucleotidyltransferases - isolation & purification ; Nucleotidyltransferases - metabolism ; PHOSPHATE ; Phosphates - metabolism ; PURIFICACION ; PURIFICATION ; regulation ; Substrate Specificity ; TRANSFERASAS ; TRANSFERASE ; Transferases</subject><ispartof>The Journal of biological chemistry, 1993-03, Vol.268 (9), p.6228-6233</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-c24dcbc6217e5f309be7f37e8cd36611e96c4a3ad13ca8647f267b799b3039e13</citedby><cites>FETCH-LOGICAL-c457t-c24dcbc6217e5f309be7f37e8cd36611e96c4a3ad13ca8647f267b799b3039e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4727392$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8384204$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kleczkowski, L.A</creatorcontrib><creatorcontrib>Villand, P</creatorcontrib><creatorcontrib>Preiss, J</creatorcontrib><creatorcontrib>Olsen, O.A</creatorcontrib><title>Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Barley (Hordeum vulgare, cv. Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 and 54 kDa, which were recognized by the respective rabbit antibodies against the small and/or large subunit of spinach leaf AGP. Substrate kinetics and product inhibition studies, carried out in the direction of ADP-glucose synthesis, suggested a sequential Iso Ordered Bi Bi kinetic mechanism for the enzyme. In addition, inhibition patterns with CrATP, a dead-end inhibitor of ATP-utilizing enzymes, were consistent with ATP (synthesis reaction) and ADP-glucose (pyrophosphorolysis reaction) binding first to different free forms of the enzyme. The AGP was potently activated by 3-phosphoglycerate (PGA) (K(a) of 5 micromolar) and inhibited by orthophosphate (P(i)), with the ratio of the two effectors playing a major role in modulating AGP activity. At low [PGA]/[P(i)] ratios, P(i) could reverse the activating effect of PGA. However, at the [PGA]/[P(i)] ratios of 1.4, or higher, some activating effect of P(i) in the presence of PGA was observed. PGA decreased the Km values for all substrates of AGP (in both the synthesis and pyrophosphorolysis directions). Properties of the barley leaf AGP are compared to those of AGP from barley seed endosperm, which is insensitive to PGA/P(i) regulation</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ADENOSINDIFOSFATO</subject><subject>ADENOSINE DIPHOSPHATE</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzymatic activity</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ESTER</subject><subject>ESTERES</subject><subject>FEUILLE</subject><subject>FOSFATOS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLUCOSA</subject><subject>GLUCOSE</subject><subject>Glucose-1-Phosphate Adenylyltransferase</subject><subject>Glyceric Acids - metabolism</subject><subject>HOJAS</subject><subject>Hordeum - enzymology</subject><subject>HORDEUM VULGARE</subject><subject>INHIBIDORES DE ENZIMAS</subject><subject>INHIBITEUR D'ENZYME</subject><subject>Kinetics</subject><subject>Nucleotidyltransferases - antagonists & inhibitors</subject><subject>Nucleotidyltransferases - isolation & purification</subject><subject>Nucleotidyltransferases - metabolism</subject><subject>PHOSPHATE</subject><subject>Phosphates - metabolism</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>regulation</subject><subject>Substrate Specificity</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>Transferases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkW1rFDEQx4Mo9Vr9AkIhiEj7YjVPm4eXpVYrFhRqwXchm53sRnY3Z3JbuW_vXu-4tw4MAzO_eWD-CJ1T8oESKj_eE8JoZVitL6i-rDkTvDLP0IoSzSte01_P0eqIvESnpfwmiwlDT9CJ5lowIlYofIsTbKLHI_jeTbGM2E0tztDNg9vENOEU8NWnH1U3zD4VwOttTus-lcXzdnBLJuQ04sblAbb44jblFuYRP85D5zJc4gHcI5RX6EVwQ4HXh3iGHj7f_Ly-re6-f_l6fXVXeVGrTeWZaH3jJaMK6sCJaUAFrkD7lktJKRjpheOupdw7LYUKTKpGGdNwwg1Qfobe7-euc_ozQ9nYMRYPw-AmSHOxqpZUU8n_C1Ipasq4XsB6D_qcSskQ7DrH0eWtpcTuhLBPQtjdly3V9kkIa5a-88OCuRmhPXYdPr_U3x3qrng3hOwmH8sRE4opbtiCvd1jfez6vzGDbWLyPYyWSW2NlYztbnyzh4JL1nV5mfNwbwQ1hDP-DzufpJY</recordid><startdate>19930325</startdate><enddate>19930325</enddate><creator>Kleczkowski, L.A</creator><creator>Villand, P</creator><creator>Preiss, J</creator><creator>Olsen, O.A</creator><general>American Society for Biochemistry and Molecular Biology</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>19930325</creationdate><title>Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves</title><author>Kleczkowski, L.A ; Villand, P ; Preiss, J ; Olsen, O.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-c24dcbc6217e5f309be7f37e8cd36611e96c4a3ad13ca8647f267b799b3039e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ADENOSINDIFOSFATO</topic><topic>ADENOSINE DIPHOSPHATE</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzymatic activity</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ESTER</topic><topic>ESTERES</topic><topic>FEUILLE</topic><topic>FOSFATOS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLUCOSA</topic><topic>GLUCOSE</topic><topic>Glucose-1-Phosphate Adenylyltransferase</topic><topic>Glyceric Acids - metabolism</topic><topic>HOJAS</topic><topic>Hordeum - enzymology</topic><topic>HORDEUM VULGARE</topic><topic>INHIBIDORES DE ENZIMAS</topic><topic>INHIBITEUR D'ENZYME</topic><topic>Kinetics</topic><topic>Nucleotidyltransferases - antagonists & inhibitors</topic><topic>Nucleotidyltransferases - isolation & purification</topic><topic>Nucleotidyltransferases - metabolism</topic><topic>PHOSPHATE</topic><topic>Phosphates - metabolism</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>regulation</topic><topic>Substrate Specificity</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kleczkowski, L.A</creatorcontrib><creatorcontrib>Villand, P</creatorcontrib><creatorcontrib>Preiss, J</creatorcontrib><creatorcontrib>Olsen, O.A</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kleczkowski, L.A</au><au>Villand, P</au><au>Preiss, J</au><au>Olsen, O.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-03-25</date><risdate>1993</risdate><volume>268</volume><issue>9</issue><spage>6228</spage><epage>6233</epage><pages>6228-6233</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Barley (Hordeum vulgare, cv. Bomi) leaf ADP-glucose pyrophosphorylase (AGP) was purified to near-homogeneity, using ammonium sulfate fractionation and heat treatment as well as ion exchange, hydrophobic, and dye-ligand chromatography. The enzyme was found to be composed of two subunit types of 51 and 54 kDa, which were recognized by the respective rabbit antibodies against the small and/or large subunit of spinach leaf AGP. Substrate kinetics and product inhibition studies, carried out in the direction of ADP-glucose synthesis, suggested a sequential Iso Ordered Bi Bi kinetic mechanism for the enzyme. In addition, inhibition patterns with CrATP, a dead-end inhibitor of ATP-utilizing enzymes, were consistent with ATP (synthesis reaction) and ADP-glucose (pyrophosphorolysis reaction) binding first to different free forms of the enzyme. The AGP was potently activated by 3-phosphoglycerate (PGA) (K(a) of 5 micromolar) and inhibited by orthophosphate (P(i)), with the ratio of the two effectors playing a major role in modulating AGP activity. At low [PGA]/[P(i)] ratios, P(i) could reverse the activating effect of PGA. However, at the [PGA]/[P(i)] ratios of 1.4, or higher, some activating effect of P(i) in the presence of PGA was observed. PGA decreased the Km values for all substrates of AGP (in both the synthesis and pyrophosphorolysis directions). Properties of the barley leaf AGP are compared to those of AGP from barley seed endosperm, which is insensitive to PGA/P(i) regulation</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8384204</pmid><doi>10.1016/S0021-9258(18)53243-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-03, Vol.268 (9), p.6228-6233 |
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| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADENOSINDIFOSFATO ADENOSINE DIPHOSPHATE Adenosine Triphosphate - metabolism Analytical, structural and metabolic biochemistry Biological and medical sciences Electrophoresis, Polyacrylamide Gel enzymatic activity Enzyme Activation Enzymes and enzyme inhibitors ESTER ESTERES FEUILLE FOSFATOS Fundamental and applied biological sciences. Psychology GLUCOSA GLUCOSE Glucose-1-Phosphate Adenylyltransferase Glyceric Acids - metabolism HOJAS Hordeum - enzymology HORDEUM VULGARE INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME Kinetics Nucleotidyltransferases - antagonists & inhibitors Nucleotidyltransferases - isolation & purification Nucleotidyltransferases - metabolism PHOSPHATE Phosphates - metabolism PURIFICACION PURIFICATION regulation Substrate Specificity TRANSFERASAS TRANSFERASE Transferases |
| title | Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves |
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