Regulation of the trehalose-6-phosphate synthase complex in Saccharomyces. I. Interconversion of forms by phosphorylation
Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained...
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Veröffentlicht in: | Current genetics 1987, Vol.11 (6/7), p.459-465 |
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creator | Panek, A.C Araujo, P.S. de Neto, V.M Panek, A.D |
description | Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained by a phosphatase treatment leading to an increase in activity. The phosphorylated, less active form of the enzyme proved to be more susceptible to activation by ATP.Mg. Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms. |
doi_str_mv | 10.1007/BF00384607 |
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Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/BF00384607</identifier><identifier>PMID: 2967122</identifier><identifier>CODEN: CUGED5</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. 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I. Interconversion of forms by phosphorylation</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><description>Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained by a phosphatase treatment leading to an increase in activity. The phosphorylated, less active form of the enzyme proved to be more susceptible to activation by ATP.Mg. Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genes</subject><subject>Genes, Fungal</subject><subject>Genes, Regulator</subject><subject>Glucosyltransferases - genetics</subject><subject>Glucosyltransferases - metabolism</subject><subject>Kinetics</subject><subject>ligases</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Multienzyme Complexes - genetics</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>regulation</subject><subject>Saccharomyces</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>species</subject><subject>Species Specificity</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0cFr1zAUB_AgjvlzevEu5iAehM68pE3Sow7nBgPBzXN5TV_WStvUpD-x__0qLfM4CATyPnwD78vYGxDnIIT59OVSCGVzLcwzdoBcyUyUVj1nBwFGZlZY9YK9TOmXECBtaU7ZqSy1ASkPbPlB98ce5y6MPHg-t8TnSC32IVGms6kNaWpxJp6WcW4xEXdhmHr6y7uR36JzLcYwLI7SOb9ezzhTdGH8QzHtkT7EIfF64VtWiMv23St24rFP9Hq_z9jd5de7i6vs5vu364vPN5mTuZgzk2tSGnKPhZU1rI8KtKXGa-WaRtUleVs3qgFwqGqs0Rpy0KBRDuqyUWfswxY7xfD7SGmuhi456nscKRxTZayAMl-X9hSEXJscCrHCjxt0MaQUyVdT7AaMSwWi-tdH9b-PFb_dU4_1QM0j3QtY5-_3OSaHvY84ui49MqPKwupiZe825jFUeB9X8vNWClACcglaFeoBfladaA</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Panek, A.C</creator><creator>Araujo, P.S. de</creator><creator>Neto, V.M</creator><creator>Panek, A.D</creator><general>Springer</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>1987</creationdate><title>Regulation of the trehalose-6-phosphate synthase complex in Saccharomyces. 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Psychology</topic><topic>Gene expression</topic><topic>Genes</topic><topic>Genes, Fungal</topic><topic>Genes, Regulator</topic><topic>Glucosyltransferases - genetics</topic><topic>Glucosyltransferases - metabolism</topic><topic>Kinetics</topic><topic>ligases</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Multienzyme Complexes - genetics</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>regulation</topic><topic>Saccharomyces</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>species</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Panek, A.C</creatorcontrib><creatorcontrib>Araujo, P.S. de</creatorcontrib><creatorcontrib>Neto, V.M</creatorcontrib><creatorcontrib>Panek, A.D</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Current genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Panek, A.C</au><au>Araujo, P.S. de</au><au>Neto, V.M</au><au>Panek, A.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of the trehalose-6-phosphate synthase complex in Saccharomyces. I. Interconversion of forms by phosphorylation</atitle><jtitle>Current genetics</jtitle><addtitle>Curr Genet</addtitle><date>1987</date><risdate>1987</risdate><volume>11</volume><issue>6/7</issue><spage>459</spage><epage>465</epage><pages>459-465</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><coden>CUGED5</coden><abstract>Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained by a phosphatase treatment leading to an increase in activity. The phosphorylated, less active form of the enzyme proved to be more susceptible to activation by ATP.Mg. Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms.</abstract><cop>Heidelberg</cop><cop>Berlin</cop><pub>Springer</pub><pmid>2967122</pmid><doi>10.1007/BF00384607</doi><tpages>7</tpages></addata></record> |
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subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Gene expression Genes Genes, Fungal Genes, Regulator Glucosyltransferases - genetics Glucosyltransferases - metabolism Kinetics ligases Molecular and cellular biology Molecular genetics Multienzyme Complexes - genetics Phosphorylation Protein Kinases - metabolism regulation Saccharomyces Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics species Species Specificity |
title | Regulation of the trehalose-6-phosphate synthase complex in Saccharomyces. I. Interconversion of forms by phosphorylation |
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